Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KWW

The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0009435	biological_process	NAD biosynthetic process
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0019674	biological_process	NAD metabolic process
A	0034213	biological_process	quinolinate catabolic process
A	0042802	molecular_function	identical protein binding
A	0070062	cellular_component	extracellular exosome
A	1902494	cellular_component	catalytic complex
B	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0009435	biological_process	NAD biosynthetic process
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019363	biological_process	pyridine nucleotide biosynthetic process
B	0019674	biological_process	NAD metabolic process
B	0034213	biological_process	quinolinate catabolic process
B	0042802	molecular_function	identical protein binding
B	0070062	cellular_component	extracellular exosome
B	1902494	cellular_component	catalytic complex
C	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0009435	biological_process	NAD biosynthetic process
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0019363	biological_process	pyridine nucleotide biosynthetic process
C	0019674	biological_process	NAD metabolic process
C	0034213	biological_process	quinolinate catabolic process
C	0042802	molecular_function	identical protein binding
C	0070062	cellular_component	extracellular exosome
C	1902494	cellular_component	catalytic complex
D	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0009435	biological_process	NAD biosynthetic process
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0019363	biological_process	pyridine nucleotide biosynthetic process
D	0019674	biological_process	NAD metabolic process
D	0034213	biological_process	quinolinate catabolic process
D	0042802	molecular_function	identical protein binding
D	0070062	cellular_component	extracellular exosome
D	1902494	cellular_component	catalytic complex
E	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0009435	biological_process	NAD biosynthetic process
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0019363	biological_process	pyridine nucleotide biosynthetic process
E	0019674	biological_process	NAD metabolic process
E	0034213	biological_process	quinolinate catabolic process
E	0042802	molecular_function	identical protein binding
E	0070062	cellular_component	extracellular exosome
E	1902494	cellular_component	catalytic complex
F	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0009435	biological_process	NAD biosynthetic process
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0019363	biological_process	pyridine nucleotide biosynthetic process
F	0019674	biological_process	NAD metabolic process
F	0034213	biological_process	quinolinate catabolic process
F	0042802	molecular_function	identical protein binding
F	0070062	cellular_component	extracellular exosome
F	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PHT A 300

Chain	Residue
A	THR137
A	HOH414
B	ARG102
A	ARG138
A	HIS160
A	ARG161
A	MET169
A	LYS171
A	GLU246
A	SER268
A	HOH407

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PHT B 300

Chain	Residue
A	ARG102
B	THR137
B	ARG138
B	HIS160
B	ARG161
B	MET169
B	LYS171
B	GLU246
B	SER268
B	HOH421

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PHT C 300

Chain	Residue
C	THR137
C	ARG138
C	HIS160
C	ARG161
C	MET169
C	LYS171
C	SER268
C	HOH401
D	ARG102

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PHT D 300

Chain	Residue
C	ARG102
D	THR137
D	ARG138
D	LYS139
D	HIS160
D	ARG161
D	MET169
D	LYS171
D	GLU246
D	SER268
D	HOH406

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PHT E 300

Chain	Residue
E	THR137
E	ARG138
E	LYS139
E	HIS160
E	ARG161
E	MET169
E	LYS171
E	HOH404
F	ARG102

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PHT F 300

Chain	Residue
E	ARG102
F	THR137
F	ARG138
F	LYS139
F	HIS160
F	ARG161
F	MET169
F	LYS171
F	GLU246
F	SER268
F	HOH404

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:26805589, ECO:0000305\|PubMed:17868694, ECO:0000305\|PubMed:24038671, ECO:0007744\|PDB:2JBM, ECO:0007744\|PDB:4KWW, ECO:0007744\|PDB:5AYY

Chain	Residue	Details
C	ARG102
D	ARG102
E	ARG102
F	ARG102
A	ARG102
B	ARG102

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:26805589, ECO:0000305\|PubMed:17868694, ECO:0000305\|PubMed:24038671, ECO:0007744\|PDB:2JBM, ECO:0007744\|PDB:4KWW, ECO:0007744\|PDB:5AYY, ECO:0007744\|PDB:5AYZ

Chain	Residue	Details
D	ARG138
D	HIS160
E	ARG138
E	HIS160
F	ARG138
F	HIS160
B	ARG138
B	HIS160
C	ARG138
C	HIS160
A	ARG138
A	HIS160

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:26805589, ECO:0000305\|PubMed:24038671, ECO:0007744\|PDB:2JBM, ECO:0007744\|PDB:4KWW, ECO:0007744\|PDB:5AYY, ECO:0007744\|PDB:5AYZ

Chain	Residue	Details
A	LYS171
B	LYS171
C	LYS171
D	LYS171
E	LYS171
F	LYS171

site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:26805589, ECO:0007744\|PDB:5AYZ

Chain	Residue	Details
B	SER248
B	GLY270
C	GLU201
C	ASP222
C	SER248
C	GLY270
D	GLU201
D	ASP222
D	SER248
D	GLY270
E	GLU201
E	ASP222
E	SER248
E	GLY270
F	GLU201
F	ASP222
F	SER248
F	GLY270
A	GLU201
A	ASP222
A	SER248
A	GLY270
B	GLU201
B	ASP222

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)