C0HK51: ATP synthase subunit alpha, mitochondrial (ATP1)

ATP synthase subunit alpha, mitochondrial (ATP1) is a 510-residue protein from Pichia angusta. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: C0HK51.

Gene
ATP1
Organism
Pichia angusta
Length
510 residues
Mean pLDDT
93.3
Model
AF-C0HK51-F1 v6
Model created
1 Aug 2025
PDB structures
3

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Model confidence (pLDDT)

The mean pLDDT of this model is 93.3 (very high 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 accurate88%
70 to 90Confident: backbone generally right10%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions0%

What pLDDT means and how to read it

Function

Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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 (PubMed:25759169). F-type ATP synthases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:27791192). 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). Subunits alpha/ATP1 and beta/ATP2 form the…

Subunit structure

F-type ATP synthases have 2 components, the catalytic core F(1) and the membrane-embedded component F(0), linked together by a central stalk and a peripheral stalk (PubMed:27791192). The central stalk, also called rotor shaft, is often seen as part of F(1) (PubMed:27791192). The peripheral stalk is seen as part of F(0). F(0) contains the membrane channel next to the rotor (PubMed:27791192).…

Subcellular location

Mitochondrion inner membrane

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
5LQZEM7.0 ÅA/B/C=1-510
5LQYEM7.8 ÅA/B/C=318-510
5LQXEM7.9 ÅA/B/C=1-510

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