2AE8

Crystal Structure of Imidazoleglycerol-phosphate Dehydratase from Staphylococcus aureus subsp. aureus N315

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0003824	molecular_function	catalytic activity
A	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
A	0005737	cellular_component	cytoplasm
A	0008652	biological_process	amino acid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0000105	biological_process	L-histidine biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
B	0005737	cellular_component	cytoplasm
B	0008652	biological_process	amino acid biosynthetic process
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0000105	biological_process	L-histidine biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
C	0005737	cellular_component	cytoplasm
C	0008652	biological_process	amino acid biosynthetic process
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0000105	biological_process	L-histidine biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
D	0005737	cellular_component	cytoplasm
D	0008652	biological_process	amino acid biosynthetic process
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0000105	biological_process	L-histidine biosynthetic process
E	0003824	molecular_function	catalytic activity
E	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
E	0005737	cellular_component	cytoplasm
E	0008652	biological_process	amino acid biosynthetic process
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0000105	biological_process	L-histidine biosynthetic process
F	0003824	molecular_function	catalytic activity
F	0004424	molecular_function	imidazoleglycerol-phosphate dehydratase activity
F	0005737	cellular_component	cytoplasm
F	0008652	biological_process	amino acid biosynthetic process
F	0016829	molecular_function	lyase activity
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1001

Chain	Residue
A	HIS36
A	HIS63
A	HIS158
A	GLU162
A	MG1003

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1002

Chain	Residue
A	HOH1156
A	HOH1163
A	HIS62
A	GLU66
A	HIS159
A	HOH1046

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1003

Chain	Residue
A	MSE96
A	GLU162
A	MG1001
A	HOH1157
A	HOH1163

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1004

Chain	Residue
B	HIS62
B	GLU66
B	HOH1018
B	HOH1154
B	HOH1160
C	HIS159

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 1005

Chain	Residue
B	HIS159
F	HIS62
F	GLU66
F	HOH1092
F	HOH1153
F	HOH1158

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 1006

Chain	Residue
A	ARG137
A	ILE141
A	HOH1081
B	PRO111
B	ILE141
B	HOH1008

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 1007

Chain	Residue
B	HIS36
B	HIS158
B	GLU162
B	HOH1159
F	HIS63

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 1008

Chain	Residue
B	HIS63
C	HIS36
C	HIS158
C	GLU162

---

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1009

Chain	Residue
C	HIS62
C	GLU66
C	HOH1036
C	HOH1155
C	HOH1164
D	HIS159

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1010

Chain	Residue
C	HIS63
D	HIS36
D	HIS158
D	GLU162
D	HOH1148

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 1011

Chain	Residue
B	HIS62
B	GLU130
B	LEU131
B	HOH1044
C	ASN156
C	HIS158

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 1012

Chain	Residue
D	HIS62
D	GLU66
D	HOH1142
F	HIS159
F	HOH1055
F	HOH1073

---

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 1013

Chain	Residue
E	HIS36
E	HIS63
E	HIS158
E	GLU162
E	HOH1203

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG E 1014

Chain	Residue
E	HIS62
E	GLU66
E	HIS159
E	HOH1200
E	HOH1201
E	HOH1202

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 1015

Chain	Residue
E	GLU98
E	GLU134
E	ARG137
E	HOH1095

---

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 1016

Chain	Residue
D	HIS63
F	HIS36
F	HIS158
F	GLU162

---

Functional Information from PROSITE/UniProt

site_id	PS00954
Number of Residues	14
Details	IGP_DEHYDRATASE_1 Imidazoleglycerol-phosphate dehydratase signature 1. VDdHHvtEdiGIVI

Chain	Residue	Details
A	VAL59-ILE72

---

site_id	PS00955
Number of Residues	13
Details	IGP_DEHYDRATASE_2 Imidazoleglycerol-phosphate dehydratase signature 2. GgNtHHeiEAiFK

Chain	Residue	Details
A	GLY154-LYS166

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O23346","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"PDB data bank","title":"Crystal structure of imidazoleglycerol-phosphate dehydratase from Staphylococcus aureus subsp. aureus N315.","authors":["Kim Y.","Quartey P.","Holzle D.","Collart F.","Joachimiak A."]}},{"source":"PDB","id":"2AE8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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