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 | 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 | 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 | 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 | 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 | 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 | 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: BINDING => ECO:0000269|PubMed:9862811 |
Chain | Residue | Details |
A | ARG105 | |
B | ASP222 | |
C | ARG105 | |
C | ARG162 | |
C | LYS172 | |
C | GLU201 | |
C | ASP222 | |
D | ARG105 | |
D | ARG162 | |
D | LYS172 | |
D | GLU201 | |
A | ARG162 | |
D | ASP222 | |
E | ARG105 | |
E | ARG162 | |
E | LYS172 | |
E | GLU201 | |
E | ASP222 | |
F | ARG105 | |
F | ARG162 | |
F | LYS172 | |
F | GLU201 | |
A | LYS172 | |
F | ASP222 | |
A | GLU201 | |
A | ASP222 | |
B | ARG105 | |
B | ARG162 | |
B | LYS172 | |
B | GLU201 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | THR138 | |
D | THR138 | |
D | SER248 | |
D | VAL269 | |
E | THR138 | |
E | SER248 | |
E | VAL269 | |
F | THR138 | |
F | SER248 | |
F | VAL269 | |
A | SER248 | |
A | VAL269 | |
B | THR138 | |
B | SER248 | |
B | VAL269 | |
C | THR138 | |
C | SER248 | |
C | VAL269 |
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 |
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 |
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 |
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 |
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 | 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 |
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 |
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 |
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 |