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3SE0

Structural characterization of the subunit A mutant F508W of the A-ATP synthase from Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0015986biological_processproton motive force-driven ATP synthesis
A0016887molecular_functionATP hydrolysis activity
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 Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 589
ChainResidue
ALEU417
AASP418
AHOH607

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 590
ChainResidue
AGLU186

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
ATRP446

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS A 592
ChainResidue
AGLU555
AARG558
AGLU562
ALYS567

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 594
ChainResidue
AVAL242
AGLN246
ALYS249
AALA507

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 595
ChainResidue
ALYS468
AGLU471
AILE475
AALA507
ATRP508

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

227561

PDB entries from 2024-11-20

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