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3IKJ

Structural characterization for the nucleotide binding ability of subunit A mutant S238A of the A1AO ATP synthase

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 MPD A 589
ChainResidue
AHIS245
AGLN246
ALYS249

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
AASP420
ALEU421
AASN431
ATRP432
ALEU433
AHOH740

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
AGLU454
AMET458
ALYS461
ALEU528
AASP532
AHOH690
AHOH691

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TRS A 592
ChainResidue
APRO551
AGLU581

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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