1GPW

Structural evidence for ammonia tunneling across the (beta/alpha)8 barrel of the imidazole glycerol phosphate synthase bienzyme complex.

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	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	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	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	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	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	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	6
Details	binding site for residue PO4 A 301

Chain	Residue
A	GLY81
A	GLY82
A	HIS84
A	ASN103
A	THR104
A	HOH425

---

site_id	AC2
Number of Residues	6
Details	binding site for residue PO4 A 302

Chain	Residue
A	ALA223
A	ALA224
A	HOH421
A	ASP176
A	GLY177
A	GLY203

---

site_id	AC3
Number of Residues	7
Details	binding site for residue PO4 C 301

Chain	Residue
C	ASP176
C	GLY177
C	GLY203
C	ALA224
C	SER225
C	HOH411
C	HOH452

---

site_id	AC4
Number of Residues	4
Details	binding site for residue PO4 C 302

Chain	Residue
C	GLY82
C	ASN103
C	THR104
C	HOH418

---

site_id	AC5
Number of Residues	3
Details	binding site for residue PO4 C 303

Chain	Residue
C	LYS37
C	GLN72
C	ASP74

---

site_id	AC6
Number of Residues	3
Details	binding site for residue PO4 E 301

Chain	Residue
E	GLY81
E	GLY82
E	THR104

---

Functional Information from SwissProt/UniProt

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

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	597
Details	Domain: {"description":"Glutamine amidotransferase type-1"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Active site: {"description":"Nucleophile"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Active site: {}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
F	GLU180
F	CYS84
F	HIS178

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
B	GLU180
B	CYS84
B	HIS178

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
D	GLU180
D	CYS84
D	HIS178

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
B	CYS84
B	HIS178

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
F	CYS84
F	HIS178

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
A	ASN11
A	ASP130

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
C	ASN11
C	ASP130

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
E	ASN11
E	ASP130

---

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1bxr

Chain	Residue	Details
D	CYS84
D	HIS178

---

site_id	MCSA1
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
A	ASN11	proton acceptor, proton donor
A	ASP130	proton acceptor, proton donor

---

site_id	MCSA2
Number of Residues	2
Details	M-CSA 753

Chain	Residue	Details
C	ASN11	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	ASN11	proton acceptor, proton donor
E	ASP130	proton acceptor, proton donor

---