2WJZ

Crystal structure of (HisH) K181A Y138A mutant of imidazoleglycerolphosphate synthase (HisH HisF) which displays constitutive glutaminase activity

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0016829	molecular_function	lyase activity
B	0000105	biological_process	L-histidine biosynthetic process
B	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
B	0004359	molecular_function	glutaminase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0008652	biological_process	amino acid biosynthetic process
B	0009382	cellular_component	imidazoleglycerol-phosphate synthase complex
B	0016763	molecular_function	pentosyltransferase activity
B	0016787	molecular_function	hydrolase activity
B	0016829	molecular_function	lyase activity
C	0000105	biological_process	L-histidine biosynthetic process
C	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0008652	biological_process	amino acid biosynthetic process
C	0016829	molecular_function	lyase activity
D	0000105	biological_process	L-histidine biosynthetic process
D	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
D	0004359	molecular_function	glutaminase activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0008652	biological_process	amino acid biosynthetic process
D	0009382	cellular_component	imidazoleglycerol-phosphate synthase complex
D	0016763	molecular_function	pentosyltransferase activity
D	0016787	molecular_function	hydrolase activity
D	0016829	molecular_function	lyase activity
E	0000105	biological_process	L-histidine biosynthetic process
E	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0008652	biological_process	amino acid biosynthetic process
E	0016829	molecular_function	lyase activity
F	0000105	biological_process	L-histidine biosynthetic process
F	0000107	molecular_function	imidazoleglycerol-phosphate synthase activity
F	0004359	molecular_function	glutaminase activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0008652	biological_process	amino acid biosynthetic process
F	0009382	cellular_component	imidazoleglycerol-phosphate synthase complex
F	0016763	molecular_function	pentosyltransferase activity
F	0016787	molecular_function	hydrolase activity
F	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 1252

Chain	Residue
A	GLY81
A	GLY82
A	ASN103
A	THR104
A	HOH2043

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 1252

Chain	Residue
C	HOH2059
C	GLY82
C	ASN103
C	THR104
C	HOH2015

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 E 1252

Chain	Residue
E	GLY82
E	ASN103
E	THR104

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Active site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
A	ASP11	proton acceptor, proton donor
A	ASP130	proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
C	ASP11	proton acceptor, proton donor
C	ASP130	proton acceptor, proton donor

---

site_id	MCSA3
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
E	ASP11	proton acceptor, proton donor
E	ASP130	proton acceptor, proton donor

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