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3QIA

Crystal structure of P-loop G237A mutant 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 Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 589
ChainResidue
AHIS245
AGLN246
ALYS249
ALYS279
AVAL479
AALA507

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 590
ChainResidue
ALEU34
AALA48

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 591
ChainResidue
AALA330

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 592
ChainResidue
APHE275

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 594
ChainResidue
AALA457
ALYS461
AHOH685

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 595
ChainResidue
AILE451
AASP452
AVAL521
AARG525
AHOH777

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 596
ChainResidue
AARG114

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ACY A 598
ChainResidue
AASP252

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 599
ChainResidue
AGLU555
AGLU562
ALYS567

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 600
ChainResidue
APRO551
AGLU581
ALYS585

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

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PDB entries from 2024-07-24

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