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MIOREX complex component 2

Reviewed
Reference proteome

AF-Q05892-F1-v4

DownloadPDB file mmCIF file Predicted aligned error

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Information

Structure viewer
Model Confidence
pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test (lDDT-Cα). It is a measure of local accuracy - for interpreting larger scale features like relative domain positions see the “predicted aligned error” plot and corresponding tutorial. Confidence bands are used to colour-code the residues in the 3D viewer. The exact pLDDT value is shown when you mouseover the structure or the sequence. It can also be found in the B-factor fields of the downloadable coordinate files.

 Very high (pLDDT > 90)
 High (90 > pLDDT > 70)
 Low (70 > pLDDT > 50)
 Very low (pLDDT < 50)
AlphaFold produces a per-residue model confidence score (pLDDT) between 0 and 100. Some regions below 50 pLDDT may be unstructured in isolation.

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SequenceNo structure available
Structure Tools
  • 15:33:46
    Mol* Plugin 4.5.0 [8/22/2024, 2:35:37 PM]
Model Confidence
pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test (lDDT-Cα). It is a measure of local accuracy - for interpreting larger scale features like relative domain positions see the “predicted aligned error” plot and corresponding tutorial. Confidence bands are used to colour-code the residues in the 3D viewer. The exact pLDDT value is shown when you mouseover the structure or the sequence. It can also be found in the B-factor fields of the downloadable coordinate files.
 Very high (pLDDT > 90)
 High (90 > pLDDT > 70)
 Low (70 > pLDDT > 50)
 Very low (pLDDT < 50)
AlphaFold produces a per-residue model confidence score (pLDDT) between 0 and 100. Some regions below 50 pLDDT may be unstructured in isolation.
Scored residueAligned residue
050100150200250050100150200250
  • 0
  • 5
  • 10
  • 15
  • 20
  • 25
  • 30
Expected position error (Ångströms)

Predicted aligned error (PAE)

Click and drag a box on the PAE viewer to select regions of the structure and highlight them on the 3D viewer.

PAE data is useful for assessing inter-domain accuracy – go to Help section below for more information.

Similar structures Discover similar structures from the Protein Data Bank (PDB) and the AlphaFold Database clustered to 50% sequence identity (AFDB50) using Foldseek.
PDB ID
and chain
DescriptionSpecies Residue
range
E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
Seq.
identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
Res.
(Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
Align
in 3D
Align in 3D
PDB ID and
chain
6zr2_P_16
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Mus musculus

Mus musculus

Residue range

1 - 377Q9DC69

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.49e-10
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
17%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.10
Align in 3D
PDB ID and
chain
6zr2_P_16
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Mus musculus

Mus musculus

Residue range

1 - 377Q9DC69

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.49e-10
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
17%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.10
Align in 3D
PDB ID and
chain
7w0h_J_9
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Sus scrofa

Sus scrofa

Residue range

31 - 371F1SL07

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
1.18e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
17.3%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.40
Align in 3D
PDB ID and
chain
7w0h_J_9
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Sus scrofa

Sus scrofa

Residue range

31 - 371F1SL07

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
1.18e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
17.3%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.40
Align in 3D
PDB ID and
chain
6ztq_P_16
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Mus musculus

Mus musculus

Residue range

1 - 377Q9DC69

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
1.25e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
15.2%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.00
Align in 3D
PDB ID and
chain
6ztq_P_16
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Mus musculus

Mus musculus

Residue range

1 - 377Q9DC69

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
1.25e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
15.2%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.00
Align in 3D
PDB ID and
chain
8esz_A9_29
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Drosophila melanogaster

Drosophila melanogaster

Residue range

1 - 416Q9VPE2

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.36e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
13.3%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.40
Align in 3D
PDB ID and
chain
8esz_A9_29
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Drosophila melanogaster

Drosophila melanogaster

Residue range

1 - 416Q9VPE2

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.36e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
13.3%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.40
Align in 3D
PDB ID and
chain
4qed_A_1
Description

SDR family oxidoreductase

SDR family oxidoreductase

Species

Staphylococcus epidermidis

Staphylococcus epidermidis

Residue range

1 - 248I6ZQW6

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.81e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
14.7%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
1.85
Align in 3D
PDB ID and
chain
7v2d_J_9
Description

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial

NADH dehydrogenase [ubiquin...

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial
Species

Sus scrofa

Sus scrofa

Residue range

36 - 406A0A287AE88

E-value
Likelihood of a match between
the query and target sequence
in a structural alignment.
The lower the E-value, the more
significant the alignment.
2.81e-9
Seq. identity
Percentage of identical
residues between aligned
sequences over the
aligned length.
17.5%
Resolution (Å)
Resolution. Indicates the level
of detail present in the 3D
structure. Smaller value means
finer details of the structure
and higher quality.
3.30
Items per page:
1 – 10 of 1806
AF-Q05892-F1
Current entry

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Aligned in 3D
Rotate and zoom structures in the 3D
viewer. Structures are aligned using alpha
carbon atoms as reference points. Once
aligned, RMSD values will appear in the
list below; lower values indicate greater
similarity between the two structures.
Toggle structures in both PDB and AFDB tables to view and align them with the entry structure in the 3D viewer. You can also download the aligned coordinates of the toggled structures and the entry structure.
Structure similarity clusterPredicted structures in the AlphaFold Protein Structure Database clustered using MMseqs2 and Foldseek. This data is provided by the AFDB Clusters.

AlphaFold database protein sequences clustered by the MMseqs2 algorithm (Steinegger M. and Soeding J., Nat. Commun. 9, 2018). Each cluster is comprised of sequences that fulfil two criteria: maintaining a maximum sequence identity of 50% and achieving a 90% bi-directional sequence overlap with the longest sequence of the cluster representative.

AFDB accession DescriptionSpecies
Sequence length
Average pLDDT
AFDB accessionAF-A0A453M9S8-F1
Unreviewed
Reference proteome
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesAegilops tauschii subsp. strangulata

Aegilops tauschii subsp. strangulata...

Aegilops tauschii subsp. strangulata
Sequence length 216 Average pLDDT 96.31
AFDB accessionAF-A0A2R6PWY7-F1
Unreviewed
Reference proteome
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesActinidia chinensis var. chinensis
Actinidia chinensis var. chinensis
Sequence length 255 Average pLDDT 95.94
AFDB accessionAF-A0A7S3GHW2-F1
Unreviewed
Description Hypothetical protein
Hypothetical protein
SpeciesPalpitomonas bilix
Palpitomonas bilix
Sequence length 236 Average pLDDT 93.06
AFDB accessionAF-M8BPD3-F1
Unreviewed
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesAegilops tauschii
Aegilops tauschii
Sequence length 269 Average pLDDT 92.56
AFDB accessionAF-A0A349BAA7-F1
Unreviewed
Reference proteome
Description Uncharacterized protein
Uncharacterized protein
SpeciesAcidimicrobiaceae bacterium
Acidimicrobiaceae bacterium
Sequence length 289 Average pLDDT 92.56
AFDB accessionAF-A0A2N9GTX5-F1
Unreviewed
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesFagus sylvatica
Fagus sylvatica
Sequence length 247 Average pLDDT 92.19
AFDB accessionAF-A0A7S2YR27-F1
Unreviewed
Description Hypothetical protein
Hypothetical protein
SpeciesAmphiprora paludosa
Amphiprora paludosa
Sequence length 265 Average pLDDT 89.25
AFDB accessionAF-A0A0M0JGH3-F1
Unreviewed
Reference proteome
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesChrysochromulina tobinii
Chrysochromulina tobinii
Sequence length 273 Average pLDDT 89
AFDB accessionAF-A0A199W256-F1
Unreviewed
Reference proteome
Description NAD(P)-bd_dom domain-containing protein

NAD(P)-bd_dom domain-containing protein ...

NAD(P)-bd_dom domain-containing protein
SpeciesAnanas comosus
Ananas comosus
Sequence length 299 Average pLDDT 88.69
AFDB accessionAF-A0A4W3HGC0-F1
Unreviewed
Reference proteome
Description 3Beta_HSD domain-containing protein
3Beta_HSD domain-containing protein
SpeciesCallorhinchus milii
Callorhinchus milii
Sequence length 278 Average pLDDT 88.56
Items per page:
1 – 10 of 503

Help

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How to interpret the Predicted Aligned Error

 

The Predicted Aligned Error (PAE) measures the confidence in the relative position of two residues within the predicted structure, providing insight into the reliability of relative position and orientations of different domains. Consider the human protein encoded by the gene GNE (Q9Y223).

GNE has two distinct domains according to experimentally determined structures in the Protein Data Bank (PDBe-KB). Does AlphaFold confidently predict their relative positions? We can use the interactive Predicted Aligned Error (PAE) plot to answer this question.

The PAE plot is not an inter-residue distance map or a contact map. Instead, the shade of green indicates the expected distance error in Ångströms (Å), ranging from 0 Å to an arbitrary cut-off of 31 Å. The colour at (x, y) corresponds to the expected distance error in the residue x’s position when the predicted and the true structures are aligned on residue y.

A dark green tile corresponds to a good prediction (low error), whereas a light green tile indicates poor prediction (high error). For example, when aligning on residue 300:

  • We’re confident in the relative position of residue 200
  • We’re not confident in the relative position of residue 600

The two low-error, dark green squares correspond to the two domains. By clicking and dragging, you can highlight these squares on the structure. If you want to remove the highlighting, click the cross icon.

When selecting an off-diagonal region, the plot visually represents the relationship between the selected ranges on the sequence and structure. The x range corresponds to the selection for scored residues, highlighted in orange, while the y range of aligned residues is highlighted in emerald green.

The high PAE values across the whole inter-domain region indicate that for this particular protein, AlphaFold does not reliably predict the relative position of the domains.

Let’s consider another inter-domain example, the human protein encoded by DIP2B (Q9P265).

In this case, we have confidence in the relative position of scored residues around 1450 when aligned with residues around 850, suggesting a packing between the small central domains.

Note that the PAE scores are asymmetrical, meaning there might be variations in PAE values between (x,y) and (y,x) positions. This is particularly relevant for loop regions with highly uncertain orientations, as seen on the DNA topoisomerase 3 (Q8T2T7).

 


Last updated

Last updated in AlphaFold DB version 2022-11-01, created with the AlphaFold Monomer v2.0 pipeline.

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If you make use of an AlphaFold prediction, please cite the following papers:
Jumper, J et al. Highly accurate protein structure prediction with AlphaFold. Nature (2021).
Varadi, M et al. AlphaFold Protein Structure Database in 2024: providing structure coverage for over 214 million protein sequences. Nucleic Acids Research (2024).
If you use data from AlphaMissense in your work, please cite the following paper:
Cheng, J et al. Accurate proteome-wide missense variant effect prediction with AlphaMissense. Science (2023).

AlphaFold Data Copyright (2022) DeepMind Technologies Limited.
AlphaMissense Copyright (2023) DeepMind Technologies Limited.

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