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2P53

Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D273N mutant complexed with N-acetyl phosphonamidate-d-glucosamine-6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006044biological_processN-acetylglucosamine metabolic process
A0006046biological_processN-acetylglucosamine catabolic process
A0008270molecular_functionzinc ion binding
A0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0019262biological_processN-acetylneuraminate catabolic process
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051289biological_processprotein homotetramerization
B0006044biological_processN-acetylglucosamine metabolic process
B0006046biological_processN-acetylglucosamine catabolic process
B0008270molecular_functionzinc ion binding
B0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0019262biological_processN-acetylneuraminate catabolic process
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051289biological_processprotein homotetramerization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17567048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17567048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-07-09

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