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4V1F

Crystal structure of a mycobacterial ATP synthase rotor ring in complex with Bedaquiline

Functional Information from GO Data
ChainGOidnamespacecontents
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
A1902600biological_processproton transmembrane transport
B0015078molecular_functionproton transmembrane transporter activity
B0015986biological_processproton motive force-driven ATP synthesis
B0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
B0045259cellular_componentproton-transporting ATP synthase complex
B1902600biological_processproton transmembrane transport
C0015078molecular_functionproton transmembrane transporter activity
C0015986biological_processproton motive force-driven ATP synthesis
C0033177cellular_componentproton-transporting two-sector ATPase complex, proton-transporting domain
C0045259cellular_componentproton-transporting ATP synthase complex
C1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00605
Number of Residues22
DetailsATPASE_C ATP synthase c subunit signature. ARQPeaqgrLfTpfFItvgLvE
ChainResidueDetails
AALA44-GLU65

237423

PDB entries from 2025-06-11

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