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4EFA

Crystal Structure of the Heterotrimeric EGChead Peripheral Stalk Complex of the Yeast Vacuolar ATPase - second conformation

Functional Information from GO Data
ChainGOidnamespacecontents
C0015078molecular_functionproton transmembrane transporter activity
C0033180cellular_componentproton-transporting V-type ATPase, V1 domain
C0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
C1902600biological_processproton transmembrane transport
E0000139cellular_componentGolgi membrane
E0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
E0000329cellular_componentfungal-type vacuole membrane
E0005515molecular_functionprotein binding
E0005773cellular_componentvacuole
E0005774cellular_componentvacuolar membrane
E0007035biological_processvacuolar acidification
E0016020cellular_componentmembrane
E0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
E0033176cellular_componentproton-transporting V-type ATPase complex
E0033178cellular_componentproton-transporting two-sector ATPase complex, catalytic domain
E0045121cellular_componentmembrane raft
E0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
E0048388biological_processendosomal lumen acidification
E0061795biological_processGolgi lumen acidification
E1902600biological_processproton transmembrane transport
G0000139cellular_componentGolgi membrane
G0000221cellular_componentvacuolar proton-transporting V-type ATPase, V1 domain
G0000329cellular_componentfungal-type vacuole membrane
G0005515molecular_functionprotein binding
G0005773cellular_componentvacuole
G0005774cellular_componentvacuolar membrane
G0007035biological_processvacuolar acidification
G0016020cellular_componentmembrane
G0016471cellular_componentvacuolar proton-transporting V-type ATPase complex
G0016887molecular_functionATP hydrolysis activity
G0033176cellular_componentproton-transporting V-type ATPase complex
G0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
G0048388biological_processendosomal lumen acidification
G0061795biological_processGolgi lumen acidification
G1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 301
ChainResidue
CLEU175
CARG258
CGLU259

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 G 201
ChainResidue
GARG25

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 G 202
ChainResidue
ELYS31
GARG25
GARG28

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 G 203
ChainResidue
GARG25
GHIS18
GSER22

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378
ChainResidueDetails
ESER2

229380

PDB entries from 2024-12-25

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