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3ND8

Structural characterization for the nucleotide binding ability 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 Residues3
DetailsBINDING SITE FOR RESIDUE MRD A 589
ChainResidue
AGLN246
ALYS249
AHOH807

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MRD A 590
ChainResidue
AHOH773
AASP420
AASN431
ATRP432
ALEU433
AHOH653
AHOH717

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD A 591
ChainResidue
ALYS198
APRO200
ATYR201
ALYS202

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 592
ChainResidue
AMET458
ALYS461
ALEU528
AASP532
AHOH720
AHOH778

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 593
ChainResidue
AARG499
AGLU500
AGLN504
AHOH622
AHOH799

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 594
ChainResidue
AALA240
ATHR241
AALA419
AHOH874

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD A 595
ChainResidue
AGLU555
AGLU562
ALYS567
AHOH855

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 596
ChainResidue
AASP252
ATYR514
APRO517
AHOH758
AHOH860

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 2024-11-06

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