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3I73

Structural characterization for the nucleotide binding ability of subunit A with ADP 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 Residues21
DetailsBINDING SITE FOR RESIDUE ADP A 589
ChainResidue
ALYS240
APRO428
AALA429
AALA483
APRO485
AGLN505
AASP506
AALA507
APHE508
AHOH781
AHOH845
ATHR241
AHOH858
AHOH859
AVAL242
ATHR243
ALEU417
AASP418
AALA419
AALA422
APHE427

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
AGLN246
ALYS249
AILE475
APHE508

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
AASP420
AASN431
ATRP432
ALEU433
AHOH648
AHOH650

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 592
ChainResidue
AMET458
ALYS461
ALEU528
AASP532
AHOH771

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS A 593
ChainResidue
AGLU183
AILE184
APRO551
AGLU581

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACY A 594
ChainResidue
APHE399
ALEU417
AHOH691

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

218196

PDB entries from 2024-04-10

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