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	0005829	cellular_component	cytosol
A	0009435	biological_process	NAD+ biosynthetic process
A	0016763	molecular_function	pentosyltransferase activity
A	0034213	biological_process	quinolinate catabolic process
A	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	0005829	cellular_component	cytosol
B	0009435	biological_process	NAD+ biosynthetic process
B	0016763	molecular_function	pentosyltransferase activity
B	0034213	biological_process	quinolinate catabolic process
B	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	0005829	cellular_component	cytosol
C	0009435	biological_process	NAD+ biosynthetic process
C	0016763	molecular_function	pentosyltransferase activity
C	0034213	biological_process	quinolinate catabolic process
C	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	0005829	cellular_component	cytosol
D	0009435	biological_process	NAD+ biosynthetic process
D	0016763	molecular_function	pentosyltransferase activity
D	0034213	biological_process	quinolinate catabolic process
D	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	0005829	cellular_component	cytosol
E	0009435	biological_process	NAD+ biosynthetic process
E	0016763	molecular_function	pentosyltransferase activity
E	0034213	biological_process	quinolinate catabolic process
E	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	0005829	cellular_component	cytosol
F	0009435	biological_process	NAD+ biosynthetic process
F	0016763	molecular_function	pentosyltransferase activity
F	0034213	biological_process	quinolinate catabolic process
F	0034354	biological_process	'de novo' NAD+ biosynthetic process from L-tryptophan
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	24
Details	Region: {"description":"Important for hexamer formation","evidences":[{"source":"PubMed","id":"26805589","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26805589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17868694","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24038671","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AYY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26805589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17868694","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24038671","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AYZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26805589","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24038671","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2JBM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KWW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AYZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26805589","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AYZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---