7khr

Electron Microscopy
3.62Å resolution

Cryo-EM structure of bafilomycin A1-bound intact V-ATPase from bovine brain

Released:
Source organism: Bos taurus
Primary publication:
Molecular basis of V-ATPase inhibition by bafilomycin A1.
OpenAccess logo Nat Commun 12 1782 (2021)
PMID: 33741963
Related structures: EMD-22880

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 32-mer (preferred)
PDBe Complex ID:
PDB-CPX-129223 (preferred)
Entry contents:
16 distinct polypeptide molecules
Macromolecules (18 distinct):
V-type proton ATPase catalytic subunit A Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 617 amino acids
Theoretical weight: 68.42 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P31404 (Residues: 1-617; Coverage: 100%)
Gene names: ATP6A1, ATP6V1A, ATP6V1A1
Sequence domains:
V-type proton ATPase subunit B, brain isoform Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 511 amino acids
Theoretical weight: 56.64 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P31408 (Residues: 1-511; Coverage: 100%)
Gene names: ATP6B2, ATP6V1B2
Sequence domains:
V-type proton ATPase subunit C 1 Chain: G
V-type proton ATPase subunit D Chain: H
V-type proton ATPase subunit E 1 Chains: I, J, K
V-type proton ATPase subunit F Chain: L
V-type proton ATPase subunit G 2 Chains: M, N, O
V-type proton ATPase subunit H Chain: P
V-type proton ATPase 116 kDa subunit a 1 Chain: a
V-type proton ATPase 21 kDa proteolipid subunit c'' Chain: b
V-type proton ATPase subunit d 1 Chain: d
V-type proton ATPase subunit e 2 Chain: e
V-type proton ATPase subunit S1 Chain: s
Renin receptor Chain: r
V-type proton ATPase 16 kDa proteolipid subunit c Chains: c, g, k, l, m, n, o, p, q
Ribonuclease kappa Chain: f

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, GLC
Carbohydrate polymer : NEW Components: MAN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 3.62Å
Relevant EMDB volumes: EMD-22880