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AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C (P25515)

Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C (P25515) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P25515
Type: protein
Length: 160 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x854ac6A396D6e8Ea3EFbfaDbB10Bb9DBe804468b
Molecule: V-type proton ATPase subunit C
UniProt: P25515

Structure

1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	V-type proton ATPase subunit C	protein	160	82% helix, 0% strand	P25515

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6PE5 · Yeast Vo motor in complex with 2 VopQ molecules · an experimental structure of the same protein · chain A against M, TM-score 0.98
6PE5 · Yeast vo motor in complex with 2 vopq molecules · an experimental structure of the same protein · chain A against I, TM-score 0.98
6C6L · Yeast Vacuolar ATPase Vo in lipid nanodisc · an experimental structure of the same protein · chain A against H, TM-score 0.98
6C6L · Yeast vacuolar ATPase vo in lipid nanodisc · an experimental structure of the same protein · chain A against H, TM-score 0.98
6PE4 · Yeast Vo motor in complex with 1 VopQ molecule · an experimental structure of the same protein · chain A against L, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P25515
Elsewhere: UniProt P25515 · AlphaFold DB P25515

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