Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QPQ

Structure of Quinolinic Acid Phosphoribosyltransferase from Mycobacterium Tuberculosis: A Potential TB Drug Target

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0009435	biological_process	NAD+ biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0034213	biological_process	quinolinate catabolic process
B	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
B	0005737	cellular_component	cytoplasm
B	0005886	cellular_component	plasma membrane
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0009435	biological_process	NAD+ biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019363	biological_process	pyridine nucleotide biosynthetic process
B	0034213	biological_process	quinolinate catabolic process
C	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0009435	biological_process	NAD+ biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0019363	biological_process	pyridine nucleotide biosynthetic process
C	0034213	biological_process	quinolinate catabolic process
D	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
D	0005737	cellular_component	cytoplasm
D	0005886	cellular_component	plasma membrane
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0009435	biological_process	NAD+ biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0019363	biological_process	pyridine nucleotide biosynthetic process
D	0034213	biological_process	quinolinate catabolic process
E	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
E	0005737	cellular_component	cytoplasm
E	0005886	cellular_component	plasma membrane
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0009435	biological_process	NAD+ biosynthetic process
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0019363	biological_process	pyridine nucleotide biosynthetic process
E	0034213	biological_process	quinolinate catabolic process
F	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
F	0005737	cellular_component	cytoplasm
F	0005886	cellular_component	plasma membrane
F	0009274	cellular_component	peptidoglycan-based cell wall
F	0009435	biological_process	NAD+ biosynthetic process
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0019363	biological_process	pyridine nucleotide biosynthetic process
F	0034213	biological_process	quinolinate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 2985

Chain	Residue
A	LYS140
A	GLY249
A	GLY270
A	ALA271
A	HIS274
A	HOH3087

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 2986

Chain	Residue
B	ALA771
B	HIS774
B	HOH3240
B	LYS640
B	GLY749
B	GLY770

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 2987

Chain	Residue
C	LYS1140
C	GLY1249
C	GLY1270
C	ALA1271
C	HIS1274
C	HOH3082

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 2988

Chain	Residue
F	LYS2640
F	GLY2749
F	GLY2770
F	HIS2774
F	HOH3071
F	HOH3227

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 E 2989

Chain	Residue
E	LYS2140
E	GLY2249
E	GLY2270
E	ALA2271
E	HIS2274
E	HOH3111
E	HOH3192

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 D 2990

Chain	Residue
D	LYS1640
D	GLY1749
D	GLY1770
D	ALA1771
D	HIS1774
D	HOH3182

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NTM A 2901

Chain	Residue
A	THR138
A	ARG139
A	LYS140
A	HIS161
A	ARG162
A	LEU170
A	LYS172
A	HOH3261
B	ARG605

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE NTM B 2902

Chain	Residue
B	THR638
B	ARG639
B	LYS640
B	HIS661
B	ARG662
B	LEU670
B	LYS672
B	LEU720
B	SER748

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NTM C 2903

Chain	Residue
C	THR1138
C	ARG1139
C	HIS1161
C	ARG1162
C	LEU1170
C	LYS1172

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NTM D 2904

Chain	Residue
D	THR1638
D	ARG1639
D	HIS1661
D	ARG1662
D	LEU1670
D	LYS1672
D	LEU1720

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NTM E 2905

Chain	Residue
E	THR2138
E	ARG2139
E	HIS2161
E	ARG2162
E	LEU2170
E	LYS2172
E	LEU2220

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NTM F 2906

Chain	Residue
F	THR2638
F	ARG2639
F	HIS2661
F	ARG2662
F	LEU2670
F	LYS2672

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9862811","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
A	ARG105
B	GLU701
B	LYS640
B	ASP722

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
A	GLU201
A	LYS140
A	ASP222
B	ARG605

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
C	ARG1105
D	LYS1640
D	GLU1701
D	ASP1722

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
D	ARG1605
C	LYS1140
C	GLU1201
C	ASP1222

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
F	GLU2701
F	ASP2722
F	LYS2640
E	ARG2105

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1qpr

Chain	Residue	Details
F	ARG2605
E	GLU2201
E	LYS2140
E	ASP2222

site_id	MCSA1
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
A	ARG105	electrostatic stabiliser
A	LYS140	electrostatic stabiliser, repulsive charge-charge interaction, steric role
A	LYS172	electrostatic stabiliser, proton acceptor, proton donor
A	GLU201	electrostatic stabiliser, proton acceptor, proton donor
A	ASP222	electrostatic stabiliser

site_id	MCSA2
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
B	ARG605	electrostatic stabiliser
B	LYS640	electrostatic stabiliser, repulsive charge-charge interaction, steric role
B	LYS672	electrostatic stabiliser, proton acceptor, proton donor
B	GLU701	electrostatic stabiliser, proton acceptor, proton donor
B	ASP722	electrostatic stabiliser

site_id	MCSA3
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
C	ARG1105	electrostatic stabiliser
C	LYS1140	electrostatic stabiliser, repulsive charge-charge interaction, steric role
C	LYS1172	electrostatic stabiliser, proton acceptor, proton donor
C	GLU1201	electrostatic stabiliser, proton acceptor, proton donor
C	ASP1222	electrostatic stabiliser

site_id	MCSA4
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
D	ARG1605	electrostatic stabiliser
D	LYS1640	electrostatic stabiliser, repulsive charge-charge interaction, steric role
D	LYS1672	electrostatic stabiliser, proton acceptor, proton donor
D	GLU1701	electrostatic stabiliser, proton acceptor, proton donor
D	ASP1722	electrostatic stabiliser

site_id	MCSA5
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
E	ARG2105	electrostatic stabiliser
E	LYS2140	electrostatic stabiliser, repulsive charge-charge interaction, steric role
E	LYS2172	electrostatic stabiliser, proton acceptor, proton donor
E	GLU2201	electrostatic stabiliser, proton acceptor, proton donor
E	ASP2222	electrostatic stabiliser

site_id	MCSA6
Number of Residues	5
Details	M-CSA 8

Chain	Residue	Details
F	ARG2605	electrostatic stabiliser
F	LYS2640	electrostatic stabiliser, repulsive charge-charge interaction, steric role
F	LYS2672	electrostatic stabiliser, proton acceptor, proton donor
F	GLU2701	electrostatic stabiliser, proton acceptor, proton donor
F	ASP2722	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)