6wlw

Electron Microscopy
3Å resolution

The Vo region of human V-ATPase in state 1 (focused refinement)

Released:
Source organism: Homo sapiens
Primary publication:
Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.
Mol Cell 80 501-511.e3 (2020)
PMID: 33065002
Related structures: EMD-21844

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
PDBe Complex ID:
PDB-CPX-127434 (preferred)
Entry contents:
8 distinct polypeptide molecules
Macromolecules (12 distinct):
V-type proton ATPase 21 kDa proteolipid subunit c'' Chain: 0
Molecule details ›
Chain: 0
Length: 205 amino acids
Theoretical weight: 21.42 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: Q99437 (Residues: 1-205; Coverage: 100%)
Gene names: ATP6F, ATP6V0B
Sequence domains: ATP synthase subunit C
V-type proton ATPase 16 kDa proteolipid subunit c Chains: 1, 2, 3, 4, 5, 6, 7, 8, 9
Molecule details ›
Chains: 1, 2, 3, 4, 5, 6, 7, 8, 9
Length: 155 amino acids
Theoretical weight: 15.74 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P27449 (Residues: 1-155; Coverage: 100%)
Gene names: ATP6C, ATP6L, ATP6V0C, ATPL
Sequence domains: ATP synthase subunit C
V-type proton ATPase subunit d 1 Chain: Q
V-type proton ATPase 116 kDa subunit a 1 Chain: R
V-type proton ATPase subunit e 1 Chain: S
Ribonuclease kappa Chain: T
V-type proton ATPase subunit S1 Chain: U
Renin receptor Chain: V

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GLC
Carbohydrate polymer : NEW Components: BGC, GAL, NGA, SIA
Carbohydrate polymer : NEW Components: GAL, NGA, SIA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution:
Relevant EMDB volumes: EMD-21844