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2P50

Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn

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
C0006040biological_processamino sugar metabolic process
C0006044biological_processN-acetylglucosamine metabolic process
C0006046biological_processN-acetylglucosamine catabolic process
C0008270molecular_functionzinc ion binding
C0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
C0016787molecular_functionhydrolase activity
C0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
C0019262biological_processN-acetylneuraminate catabolic process
C0032991cellular_componentprotein-containing complex
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
C0051289biological_processprotein homotetramerization
D0006040biological_processamino sugar metabolic process
D0006044biological_processN-acetylglucosamine metabolic process
D0006046biological_processN-acetylglucosamine catabolic process
D0008270molecular_functionzinc ion binding
D0008448molecular_functionN-acetylglucosamine-6-phosphate deacetylase activity
D0016787molecular_functionhydrolase activity
D0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
D0019262biological_processN-acetylneuraminate catabolic process
D0032991cellular_componentprotein-containing complex
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0047419molecular_functionN-acetylgalactosamine-6-phosphate deacetylase activity
D0051289biological_processprotein homotetramerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AGLU131
AHIS195
AHIS216
AHOH690

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 601
ChainResidue
BGLU131
BHIS195
BHIS216
BHOH696

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 601
ChainResidue
CHIS195
CHIS216
CHOH688
CGLU131

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 601
ChainResidue
DGLU131
DHIS195
DHIS216
DHOH679

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17567048
ChainResidueDetails
AASP273
BASP273
CASP273
DASP273

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:17567048
ChainResidueDetails
AGLU131
AASN219
AARG227
AASP248
ALEU306
BGLU131
BTHR142
BHIS195
BHIS216
BASN219
BARG227
BASP248
BLEU306
CGLU131
CTHR142
CHIS195
CHIS216
CASN219
CARG227
CASP248
CLEU306
DGLU131
DTHR142
DHIS195
DHIS216
DASN219
DARG227
DASP248
DLEU306
ATHR142
AHIS195
AHIS216

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PDB entries from 2024-06-12

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