P03929: ATP synthase F(0) complex subunit 8 (MT-ATP8)

ATP synthase F(0) complex subunit 8 (MT-ATP8) is a 66-residue protein from Bos taurus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P03929.

Gene
MT-ATP8
Organism
Bos taurus
Length
66 residues
Mean pLDDT
74.9
Model
AF-P03929-F1 v6
Model created
1 Aug 2025
PDB structures
19

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Model confidence (pLDDT)

The mean pLDDT of this model is 74.9 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate24%
70 to 90Confident: backbone generally right26%
50 to 70Low: treat with caution50%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Subunit 8, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can…

Subunit structure

Component of the ATP synthase complex composed at least of ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c (homooctamer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e, ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j, ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon, ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d,…

Subcellular location

Mitochondrion membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6ZQMEM3.29 Å8=1-66
9W2REM3.4 Å8=1-66
6ZITEM3.49 Å8=1-66
6ZBBEM3.61 Å8=1-66
6ZPOEM4.0 Å8=1-66
6ZQNEM4.0 Å8=1-66
9W2SEM4.0 Å8=1-66
9W2TEM4.1 Å8=1-41
6ZIQEM4.33 Å8=1-66
6ZIUEM6.02 Å8=1-66
7AJFEM8.45 Å8/A8=1-66
7AJDEM9.0 Å8/A8=1-66
7AJBEM9.2 Å8/A8=1-66
7AJEEM9.4 Å8/A8=1-66
7AJHEM9.7 Å8/A8=1-66
7AJGEM10.7 Å8/A8=1-66
7AJIEM11.4 Å8/A8=1-66
7AJCEM11.9 Å8/A8=1-66
7AJJEM13.1 Å8/A8=1-66

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