1QPR

QUINOLINATE PHOSPHORIBOSYLTRANSFERASE (QAPRTASE) FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH PHTHALATE AND PRPCP

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 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

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

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
A	GLU201
A	LYS140
A	ASP222
B	ARG105

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site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
A	ARG105
B	GLU201
B	LYS140
B	ASP222

---

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
C	ARG105
D	GLU201
D	LYS140
D	ASP222

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site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
D	ARG105
C	GLU201
C	LYS140
C	ASP222

---

site_id	CSA5
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
F	GLU201
F	LYS140
F	ASP222
E	ARG105

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site_id	CSA6
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 9016724, 9862811

Chain	Residue	Details
F	ARG105
E	GLU201
E	LYS140
E	ASP222

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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

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 8

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

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 8

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

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site_id	MCSA4
Number of Residues	5
Details	M-CSA 8

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

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site_id	MCSA5
Number of Residues	5
Details	M-CSA 8

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

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site_id	MCSA6
Number of Residues	5
Details	M-CSA 8

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

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