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3ND9

Structural characterization for the nucleotide binding ability of subunit A of the A1AO ATP synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0015986biological_processproton motive force-driven ATP synthesis
A0033178cellular_componentproton-transporting two-sector ATPase complex, catalytic domain
A0046034biological_processATP metabolic process
A0046961molecular_functionproton-transporting ATPase activity, rotational mechanism
A1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD A 589
ChainResidue
AASP420
AASN431
ATRP432
ALEU433

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MRD A 590
ChainResidue
AILE451
AASP452

Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINWLTSYS
ChainResidueDetails
APRO428-SER437

218853

PDB entries from 2024-04-24

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