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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
A0006040biological_processamino sugar metabolic process
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
A0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
A0051289biological_processprotein homotetramerization
B0006040biological_processamino sugar metabolic process
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
B0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
B0051289biological_processprotein homotetramerization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17567048
ChainResidueDetails
AASN273
BASN273

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:17567048
ChainResidueDetails
AGLU131
AHIS195
AHIS216
AASN219
AARG227
AASP248
ALEU306
BGLU131
BTHR142
BHIS195
BHIS216
BASN219
BARG227
BASP248
BLEU306
ATHR142

221051

PDB entries from 2024-06-12

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