1YRR

Crystal Structure Of The N-Acetylglucosamine-6-Phosphate Deacetylase From Escherichia Coli K12 at 2.0 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006040	biological_process	amino sugar metabolic process
A	0006044	biological_process	N-acetylglucosamine metabolic process
A	0006046	biological_process	N-acetylglucosamine catabolic process
A	0008270	molecular_function	zinc ion binding
A	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0019262	biological_process	N-acetylneuraminate catabolic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0047419	molecular_function	N-acetylgalactosamine-6-phosphate deacetylase activity
A	0051289	biological_process	protein homotetramerization
B	0006040	biological_process	amino sugar metabolic process
B	0006044	biological_process	N-acetylglucosamine metabolic process
B	0006046	biological_process	N-acetylglucosamine catabolic process
B	0008270	molecular_function	zinc ion binding
B	0008448	molecular_function	N-acetylglucosamine-6-phosphate deacetylase activity
B	0016787	molecular_function	hydrolase activity
B	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B	0019262	biological_process	N-acetylneuraminate catabolic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0047419	molecular_function	N-acetylgalactosamine-6-phosphate deacetylase activity
B	0051289	biological_process	protein homotetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 501

Chain	Residue
A	GLN59
A	GLU131
A	HIS195
A	HIS216
A	ASP273
A	HOH858
A	HOH860

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 502

Chain	Residue
B	HIS195
B	HIS216
B	ASP273
B	HOH672
B	ASN61
B	GLU131

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 601

Chain	Residue
A	THR225
A	GLY226
A	ARG227
A	GLU228
B	TYR223

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site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 602

Chain	Residue
A	ASP253
A	ALA255
A	ARG258
A	HIS323
A	HOH862
A	HOH865
A	HOH866
B	LEU200

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 603

Chain	Residue
A	LYS261
A	ARG262
A	GLY265
A	HOH863
A	HOH864

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17567048

Chain	Residue	Details
A	ASP273
B	ASP273

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site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:17567048

Chain	Residue	Details
A	GLU131
B	THR142
B	HIS195
B	HIS216
B	ASN219
B	ARG227
B	ASP248
B	LEU306
A	THR142
A	HIS195
A	HIS216
A	ASN219
A	ARG227
A	ASP248
A	LEU306
B	GLU131

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