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Crystal structure of subunit C (VMA5P) of the yeast V-ATPase

Analyse Crystal structure of subunit C (VMA5P) of the yeast V-ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U7L
Type: protein
Length: 364 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Vacuolar ATP synthase subunit C
EC: 3.6.3.14
UniProt: P31412
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Vacuolar ATP synthase subunit C (EC 3.6.3.14)	protein	364	52% helix, 16% strand	P31412

Ligands and binding sites

TLA · L(+)-tartaric acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.36	0.75	21	empty
2	59	0.31	0.76	17	empty

Compared structures

1U7L · Crystal Structure of subunit C (vma5p) of the yeast V-ATPase · the same entry in another collection · chain A against A, TM-score 1.00
P31412 · AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C (P31412) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P31412
Elsewhere: RCSB PDB 1U7L · PDBe 1U7L · UniProt P31412

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