Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QPN

Quinolinate Phosphoribosyl Transferase from Mycobacterium Tuberculosis in Complex with NCNN

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	15
Details	BINDING SITE FOR RESIDUE NCN A 2901

Chain	Residue
A	THR138
A	ALA268
A	GLY270
A	ALA271
A	HIS274
A	HOH3014
A	HOH3168
A	ARG139
A	LYS140
A	HIS161
A	ARG162
A	LEU220
A	ASP222
A	SER248
A	GLY249

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE NCN B 2902

Chain	Residue
B	THR638
B	ARG639
B	LYS640
B	HIS661
B	ARG662
B	LEU720
B	ASP722
B	SER748
B	GLY749
B	ALA768
B	GLY770
B	ALA771
B	HIS774
B	HOH3031
B	HOH3246

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NCN E 2903

Chain	Residue
E	THR2138
E	LYS2140
E	HIS2161
E	ARG2162
E	LEU2220
E	ASP2222
E	SER2248
E	GLY2249
E	ALA2268
E	GLY2270
E	ALA2271
E	HIS2274
E	HOH3006
E	HOH3120
E	HOH3198
E	HOH3227

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NCN D 2904

Chain	Residue
D	THR1638
D	LYS1640
D	HIS1661
D	ARG1662
D	LEU1720
D	ASP1722
D	SER1748
D	GLY1749
D	ALA1768
D	GLY1770
D	ALA1771
D	HIS1774
D	HOH3008
D	HOH3108

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE NCN C 2905

Chain	Residue
C	THR1138
C	LYS1140
C	HIS1161
C	ARG1162
C	LEU1220
C	ASP1222
C	SER1248
C	GLY1249
C	ALA1268
C	GLY1270
C	ALA1271
C	HIS1274
C	HOH3005
C	HOH3116
C	HOH3177
C	HOH3188

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE NCN F 2906

Chain	Residue
F	THR2638
F	ARG2639
F	LYS2640
F	HIS2661
F	ARG2662
F	ASP2722
F	SER2748
F	GLY2749
F	ALA2768
F	GLY2770
F	ALA2771
F	HIS2774
F	HOH3101

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)