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3M4Y

Structural characterization of the subunit A mutant P235A of the A-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 Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 589
ChainResidue
ALYS198
APRO200
ATYR201
ALYS202

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 590
ChainResidue
AALA464
ALEU465
ALYS468
ATYR531
AHOH879

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 591
ChainResidue
AASP420
AASN431
ATRP432
ALEU433
AHOH683
AHOH743

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS A 592
ChainResidue
AGLU454
AMET458
ALYS461
AASN529
AASP532
AHOH713

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY A 593
ChainResidue
ALYS198
AHOH1007

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 594
ChainResidue
AGLU161
AVAL173
AILE174
AALA175
AHOH783
AHOH898

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 595
ChainResidue
AHIS245
AGLN246
ALYS249
ALEU278

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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