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1RY2

Crystal structure of yeast acetyl-coenzyme A synthetase in complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003987molecular_functionacetate-CoA ligase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006085biological_processacetyl-CoA biosynthetic process
A0016208molecular_functionAMP binding
A0016874molecular_functionligase activity
A0016880molecular_functionacid-ammonia (or amide) ligase activity
A0019427biological_processacetyl-CoA biosynthetic process from acetate
A0019654biological_processpyruvate fermentation to acetate
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP A 720
ChainResidue
AILE366
ATHR472
AASP559
AILE571
AARG574
AGLY443
AGLU444
APRO445
AASP467
ATHR468
ATYR469
ATRP470
AGLN471

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LLYTSGSTGaPK
ChainResidueDetails
ALEU317-LYS328

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsMotif: {"description":"FACS","evidences":[{"source":"UniProtKB","id":"P30624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsMotif: {"description":"Microbody targeting signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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