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3I72

Structural characterization for the nucleotide binding ability of subunit A with SO4 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 Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 592
ChainResidue
AHOH754
AHOH771
AHOH885
AHOH896

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE TRS A 593
ChainResidue
AILE184
AGLU581

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 594
ChainResidue
AGLU161
AALA163
AVAL173

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 589
ChainResidue
AGLN246
ALYS249
AVAL479

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
AMET458
ALYS461
ALEU528
AASP532
AHOH774

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
AASP420
ALEU421
ATRP432
ALEU433
AHOH688
AHOH720

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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