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4RND

Crystal Structure of the subunit DF-assembly of the eukaryotic V-ATPase.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
A0000329cellular_componentfungal-type vacuole membrane
A0005515molecular_functionprotein binding
A0005773cellular_componentvacuole
A0005774cellular_componentvacuolar membrane
A0006811biological_processmonoatomic ion transport
A0007035biological_processvacuolar acidification
A0016020cellular_componentmembrane
A0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
A0033176cellular_componentproton-transporting V-type ATPase complex
A0045121cellular_componentmembrane raft
A0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
A0048388biological_processendosomal lumen acidification
A0061795biological_processGolgi lumen acidification
A1902600biological_processproton transmembrane transport
B0000139cellular_componentGolgi membrane
B0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
B0000329cellular_componentfungal-type vacuole membrane
B0005515molecular_functionprotein binding
B0005773cellular_componentvacuole
B0005774cellular_componentvacuolar membrane
B0006811biological_processmonoatomic ion transport
B0007035biological_processvacuolar acidification
B0016020cellular_componentmembrane
B0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
B0033176cellular_componentproton-transporting V-type ATPase complex
B0033180cellular_componentproton-transporting V-type ATPase, V1 domain
B0034220biological_processmonoatomic ion transmembrane transport
B0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
B0048388biological_processendosomal lumen acidification
B0061795biological_processGolgi lumen acidification
B1902600biological_processproton transmembrane transport
C0000139cellular_componentGolgi membrane
C0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
C0000329cellular_componentfungal-type vacuole membrane
C0005515molecular_functionprotein binding
C0005773cellular_componentvacuole
C0005774cellular_componentvacuolar membrane
C0006811biological_processmonoatomic ion transport
C0007035biological_processvacuolar acidification
C0016020cellular_componentmembrane
C0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
C0033176cellular_componentproton-transporting V-type ATPase complex
C0045121cellular_componentmembrane raft
C0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
C0048388biological_processendosomal lumen acidification
C0061795biological_processGolgi lumen acidification
C1902600biological_processproton transmembrane transport
D0000139cellular_componentGolgi membrane
D0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
D0000329cellular_componentfungal-type vacuole membrane
D0005515molecular_functionprotein binding
D0005773cellular_componentvacuole
D0005774cellular_componentvacuolar membrane
D0006811biological_processmonoatomic ion transport
D0007035biological_processvacuolar acidification
D0016020cellular_componentmembrane
D0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
D0033176cellular_componentproton-transporting V-type ATPase complex
D0033180cellular_componentproton-transporting V-type ATPase, V1 domain
D0034220biological_processmonoatomic ion transmembrane transport
D0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
D0048388biological_processendosomal lumen acidification
D0061795biological_processGolgi lumen acidification
D1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
ASER88
ATHR89
AASN118
APHE120
AHOH418
BLEU21
BGLY26

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 201
ChainResidue
BHIS56
BHOH308
CTYR81
BGLU34
BLYS53

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL C 301
ChainResidue
CASN183
CTHR184
CHOH406
CHOH407
CHOH409

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PDB entries from 2025-07-23

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