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 |
