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8W0M

Crystal structure of Acetyl-CoA synthetase 2 from Candida albicans in complex with a Acetyl Sulfamate AMP ester inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003987molecular_functionacetate-CoA ligase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006085biological_processacetyl-CoA biosynthetic process
A0016208molecular_functionAMP binding
A0016874molecular_functionligase activity
A0019427biological_processacetyl-CoA biosynthetic process from acetate
B0000166molecular_functionnucleotide binding
B0003987molecular_functionacetate-CoA ligase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006085biological_processacetyl-CoA biosynthetic process
B0016208molecular_functionAMP binding
B0016874molecular_functionligase activity
B0019427biological_processacetyl-CoA biosynthetic process from acetate
C0000166molecular_functionnucleotide binding
C0003987molecular_functionacetate-CoA ligase activity
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0006085biological_processacetyl-CoA biosynthetic process
C0016208molecular_functionAMP binding
C0016874molecular_functionligase activity
C0019427biological_processacetyl-CoA biosynthetic process from acetate
Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LLYTSGSTGtPK
ChainResidueDetails
ALEU291-LYS302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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