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3I4L

Structural characterization for the nucleotide binding ability of subunit A with AMP-PNP 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 Residues21
DetailsBINDING SITE FOR RESIDUE ANP A 589
ChainResidue
APRO233
AALA419
AALA422
APHE427
APRO428
AALA429
AALA483
APRO485
AGLN505
AASP506
AALA507
APRO235
APHE508
AHOH685
ASER238
ALYS240
ATHR241
AVAL242
ATHR243
ALEU417
AASP418

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MPD A 592
ChainResidue
AGLN246
ALYS249

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
AASP420
ALEU421
AARG424
AASN431
ATRP432
ALEU433
AHOH793

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
AMET458
ALYS461
AARG525
ALEU528
AASP532
AHOH610

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 593
ChainResidue
AGLU161
AILE162
AALA163
AVAL173
AILE174

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS A 594
ChainResidue
AGLU183
AILE184
ALEU550
APRO551
AGLU581
AHOH948

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

237735

PDB entries from 2025-06-18

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