3RV9

Structure of a M. tuberculosis Salicylate Synthase, MbtI, in Complex with an Inhibitor with Ethyl R-Group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000162	biological_process	tryptophan biosynthetic process
A	0000287	molecular_function	magnesium ion binding
A	0004106	molecular_function	chorismate mutase activity
A	0005886	cellular_component	plasma membrane
A	0008909	molecular_function	isochorismate synthase activity
A	0009058	biological_process	biosynthetic process
A	0009697	biological_process	salicylic acid biosynthetic process
A	0010106	biological_process	cellular response to iron ion starvation
A	0016829	molecular_function	lyase activity
A	0016833	molecular_function	oxo-acid-lyase activity
A	0016853	molecular_function	isomerase activity
A	0019540	biological_process	catechol-containing siderophore biosynthetic process
A	0043904	molecular_function	isochorismate pyruvate lyase activity
A	0046872	molecular_function	metal ion binding
A	0052572	biological_process	response to host immune response
B	0000162	biological_process	tryptophan biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0004106	molecular_function	chorismate mutase activity
B	0005886	cellular_component	plasma membrane
B	0008909	molecular_function	isochorismate synthase activity
B	0009058	biological_process	biosynthetic process
B	0009697	biological_process	salicylic acid biosynthetic process
B	0010106	biological_process	cellular response to iron ion starvation
B	0016829	molecular_function	lyase activity
B	0016833	molecular_function	oxo-acid-lyase activity
B	0016853	molecular_function	isomerase activity
B	0019540	biological_process	catechol-containing siderophore biosynthetic process
B	0043904	molecular_function	isochorismate pyruvate lyase activity
B	0046872	molecular_function	metal ion binding
B	0052572	biological_process	response to host immune response
C	0000162	biological_process	tryptophan biosynthetic process
C	0000287	molecular_function	magnesium ion binding
C	0004106	molecular_function	chorismate mutase activity
C	0005886	cellular_component	plasma membrane
C	0008909	molecular_function	isochorismate synthase activity
C	0009058	biological_process	biosynthetic process
C	0009697	biological_process	salicylic acid biosynthetic process
C	0010106	biological_process	cellular response to iron ion starvation
C	0016829	molecular_function	lyase activity
C	0016833	molecular_function	oxo-acid-lyase activity
C	0016853	molecular_function	isomerase activity
C	0019540	biological_process	catechol-containing siderophore biosynthetic process
C	0043904	molecular_function	isochorismate pyruvate lyase activity
C	0046872	molecular_function	metal ion binding
C	0052572	biological_process	response to host immune response
D	0000162	biological_process	tryptophan biosynthetic process
D	0000287	molecular_function	magnesium ion binding
D	0004106	molecular_function	chorismate mutase activity
D	0005886	cellular_component	plasma membrane
D	0008909	molecular_function	isochorismate synthase activity
D	0009058	biological_process	biosynthetic process
D	0009697	biological_process	salicylic acid biosynthetic process
D	0010106	biological_process	cellular response to iron ion starvation
D	0016829	molecular_function	lyase activity
D	0016833	molecular_function	oxo-acid-lyase activity
D	0016853	molecular_function	isomerase activity
D	0019540	biological_process	catechol-containing siderophore biosynthetic process
D	0043904	molecular_function	isochorismate pyruvate lyase activity
D	0046872	molecular_function	metal ion binding
D	0052572	biological_process	response to host immune response

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RVD A 451

Chain	Residue
A	PRO251
A	THR361
A	TYR385
A	LEU404
A	ARG405
A	ALA418
A	GLY419
A	LYS438
A	HOH538

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE RVD B 451

Chain	Residue
B	LEU268
B	THR271
B	HIS334
B	THR361
B	TYR385
B	ARG405
B	ALA418
B	GLY419
B	LYS438
B	HOH521

---

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RVD C 451

Chain	Residue
C	GLU252
C	THR361
C	TYR385
C	LEU404
C	ARG405
C	ALA418
C	GLY419
C	LYS438
C	HOH505

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE RVD D 451

Chain	Residue
D	PRO251
D	THR361
D	TYR385
D	LEU404
D	ARG405
D	ALA418
D	GLY419
D	LYS438
D	HOH506

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9X9I8

Chain	Residue	Details
A	GLU252
B	GLU252
C	GLU252
D	GLU252

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697

Chain	Residue	Details
A	GLY270
B	GLY270
C	GLY270
D	GLY270

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:20512795

Chain	Residue	Details
A	GLU297
D	GLU297
D	GLU431
D	GLU434
A	GLU431
A	GLU434
B	GLU297
B	GLU431
B	GLU434
C	GLU297
C	GLU431
C	GLU434

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:16923875, ECO:0000269|PubMed:20512795, ECO:0000269|PubMed:22607697

Chain	Residue	Details
A	TYR385
C	ARG405
C	GLY419
C	LYS438
D	TYR385
D	ARG405
D	GLY419
D	LYS438
A	ARG405
A	GLY419
A	LYS438
B	TYR385
B	ARG405
B	GLY419
B	LYS438
C	TYR385

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Could activate a water molecule for attack at the C2 of chorismate and involved in recognition/elimination of the C4 hydroxyl => ECO:0000269|PubMed:17240979

Chain	Residue	Details
A	LEU268
B	LEU268
C	LEU268
D	LEU268

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