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1WU0

Solution structure of subunit c of F1Fo-ATP synthase from the thermophilic bacillus PS3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006754biological_processATP biosynthetic process
A0006811biological_processmonoatomic ion transport
A0008289molecular_functionlipid binding
A0015078molecular_functionproton transmembrane transporter activity
A0015986biological_processproton motive force-driven ATP synthesis
A0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
A0045259cellular_componentproton-transporting ATP synthase complex
A0046933molecular_functionproton-transporting ATP synthase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARQPelrpvLqTtmFIgvaLvE
ChainResidueDetails
AALA35-GLU56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reversibly protonated during proton transport"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"6447066","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1c17
ChainResidueDetails
AGLU56

247536

PDB entries from 2026-01-14

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