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5X09

Crystal structure of subunit A mutant P235A/S238C of the A-ATP synthase from pyrococcus horikoshii OT3

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
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue ACY A 601
ChainResidue
ALYS468

site_idAC2
Number of Residues3
Detailsbinding site for residue TRS A 603
ChainResidue
AGLU183
AILE184
AGLU581

site_idAC3
Number of Residues7
Detailsbinding site for residue MPD A 604
ChainResidue
AILE475
AALA507
AVAL242
AHIS245
AGLN246
ALYS249
ALEU278

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

219140

PDB entries from 2024-05-01

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