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9KYH

Crystal structure of E.coli ac4C amidohydrolase YqfB in complex with ac4C

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0016787molecular_functionhydrolase activity
A0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A0046135biological_processpyrimidine nucleoside catabolic process
A0106251molecular_functionN4-acetylcytidine amidohydrolase activity
B0005829cellular_componentcytosol
B0016787molecular_functionhydrolase activity
B0016813molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B0046135biological_processpyrimidine nucleoside catabolic process
B0106251molecular_functionN4-acetylcytidine amidohydrolase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues190
DetailsDomain: {"description":"ASCH","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31964920","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31964920","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00684","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31964920","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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