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8H9N

Human ATP synthase state 3a subregion 2

Functional Information from GO Data
ChainGOidnamespacecontents
K0000276cellular_componentmitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
K0015078molecular_functionproton transmembrane transporter activity
K0015986biological_processproton motive force-driven ATP synthesis
L0000276cellular_componentmitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
L0005515molecular_functionprotein binding
L0005739cellular_componentmitochondrion
L0005743cellular_componentmitochondrial inner membrane
L0005753cellular_componentmitochondrial proton-transporting ATP synthase complex
L0015078molecular_functionproton transmembrane transporter activity
L0015986biological_processproton motive force-driven ATP synthesis
L0021762biological_processsubstantia nigra development
L0042776biological_processproton motive force-driven mitochondrial ATP synthesis
L0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
L0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
L1902600biological_processproton transmembrane transport
M0000274cellular_componentmitochondrial proton-transporting ATP synthase, stator stalk
M0000276cellular_componentmitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
M0005515molecular_functionprotein binding
M0005739cellular_componentmitochondrion
M0005743cellular_componentmitochondrial inner membrane
M0005753cellular_componentmitochondrial proton-transporting ATP synthase complex
M0015078molecular_functionproton transmembrane transporter activity
M0015986biological_processproton motive force-driven ATP synthesis
M0042776biological_processproton motive force-driven mitochondrial ATP synthesis
M0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
M0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
M1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:25944712
ChainResidueDetails
MALA1
LLYS46
LLYS105

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9DCX2
ChainResidueDetails
MLYS31
MLYS62
MLYS71
KLYS202

site_idSWS_FT_FI3
Number of Residues5
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9DCX2
ChainResidueDetails
MLYS77
MLYS84
MLYS94
MLYS143
MLYS148

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
MLYS116
LLYS99

222036

PDB entries from 2024-07-03

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