1N3I
Crystal Structure of Mycobacterium tuberculosis PNP with transition state analog DADMe-ImmH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 301 |
| Chain | Residue |
| A | GLY35 |
| A | HOH561 |
| A | SER36 |
| A | HIS68 |
| A | ARG88 |
| A | HIS90 |
| A | ASN119 |
| A | ALA120 |
| A | SER208 |
| A | DIH401 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 302 |
| Chain | Residue |
| B | GLY35 |
| B | SER36 |
| B | HIS68 |
| B | ARG88 |
| B | HIS90 |
| B | ASN119 |
| B | ALA120 |
| B | SER208 |
| B | DIH402 |
| B | HOH532 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 C 303 |
| Chain | Residue |
| C | GLY35 |
| C | SER36 |
| C | HIS68 |
| C | ARG88 |
| C | HIS90 |
| C | ASN119 |
| C | ALA120 |
| C | SER208 |
| C | DIH403 |
| C | HOH610 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DIH A 401 |
| Chain | Residue |
| A | HIS90 |
| A | TYR92 |
| A | ALA120 |
| A | ALA121 |
| A | GLY122 |
| A | TYR188 |
| A | GLU189 |
| A | VAL205 |
| A | GLY206 |
| A | MET207 |
| A | THR230 |
| A | ASN231 |
| A | HIS243 |
| A | VAL246 |
| A | PO4301 |
| A | HOH601 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DIH B 402 |
| Chain | Residue |
| B | HIS90 |
| B | TYR92 |
| B | ALA120 |
| B | ALA121 |
| B | GLY122 |
| B | TYR188 |
| B | GLU189 |
| B | VAL205 |
| B | GLY206 |
| B | MET207 |
| B | THR230 |
| B | ASN231 |
| B | HIS243 |
| B | VAL246 |
| B | PO4302 |
| B | HOH621 |
| C | PHE153 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DIH C 403 |
| Chain | Residue |
| C | SER36 |
| C | HIS90 |
| C | TYR92 |
| C | ALA120 |
| C | ALA121 |
| C | GLY122 |
| C | TYR188 |
| C | GLU189 |
| C | VAL205 |
| C | GLY206 |
| C | MET207 |
| C | THR230 |
| C | ASN231 |
| C | HIS243 |
| C | VAL246 |
| C | PO4303 |
| C | HOH520 |
Functional Information from PROSITE/UniProt
| site_id | PS01240 |
| Number of Residues | 42 |
| Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. LvlaGriHaYeghdLryvVhpVrAaraaGaqi.MVltNAaGGL |
| Chain | Residue | Details |
| A | LEU83-LEU124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80 |
| Chain | Residue | Details |
| A | SER36 | |
| C | SER36 | |
| C | ARG88 | |
| C | SER208 | |
| A | ARG88 | |
| A | SER208 | |
| B | SER36 | |
| B | ARG88 | |
| B | SER208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P45563 |
| Chain | Residue | Details |
| A | ALA120 | |
| A | HIS68 | |
| B | ALA120 | |
| C | HIS68 | |
| C | ALA120 | |
| B | HIS68 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11444966 |
| Chain | Residue | Details |
| B | ASN231 | |
| C | GLU189 | |
| C | ASN231 | |
| A | GLU189 | |
| A | ASN231 | |
| B | GLU189 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | ARG108 | |
| B | ARG108 | |
| C | ARG108 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16460002 |
| Chain | Residue | Details |
| C | HIS211 | |
| C | PRO240 | |
| C | ALA248 | |
| A | VAL101 | |
| A | HIS211 | |
| A | PRO240 | |
| A | ALA248 | |
| B | VAL101 | |
| B | HIS211 | |
| B | PRO240 | |
| B | ALA248 | |
| C | VAL101 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 15 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU142 | |
| A | ARG217 | |
| B | ARG125 | |
| B | ASP138 | |
| B | HIS139 | |
| B | LEU142 | |
| B | ARG217 | |
| C | ARG125 | |
| C | ASP138 | |
| C | HIS139 | |
| C | LEU142 | |
| C | ARG217 | |
| A | ARG125 | |
| A | ASP138 | |
| A | HIS139 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 229 |
| Chain | Residue | Details |
| A | VAL101 | electrostatic stabiliser |
| A | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
| A | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
| A | ASP138 | metal ligand |
| A | HIS139 | metal ligand |
| A | LEU142 | metal ligand |
| A | THR213 | electrostatic stabiliser |
| A | ALA249 | electrostatic stabiliser, hydrogen bond donor |
| A | GLY250 | electrostatic stabiliser, hydrogen bond donor |
| A | ALA251 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 229 |
| Chain | Residue | Details |
| B | VAL101 | electrostatic stabiliser |
| B | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
| B | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
| B | ASP138 | metal ligand |
| B | HIS139 | metal ligand |
| B | LEU142 | metal ligand |
| B | THR213 | electrostatic stabiliser |
| B | ALA249 | electrostatic stabiliser, hydrogen bond donor |
| B | GLY250 | electrostatic stabiliser, hydrogen bond donor |
| B | ALA251 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 10 |
| Details | M-CSA 229 |
| Chain | Residue | Details |
| C | VAL101 | electrostatic stabiliser |
| C | ARG105 | electrostatic stabiliser, hydrogen bond donor, van der waals interaction |
| C | ARG108 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, van der waals interaction |
| C | ASP138 | metal ligand |
| C | HIS139 | metal ligand |
| C | LEU142 | metal ligand |
| C | THR213 | electrostatic stabiliser |
| C | ALA249 | electrostatic stabiliser, hydrogen bond donor |
| C | GLY250 | electrostatic stabiliser, hydrogen bond donor |
| C | ALA251 | electrostatic stabiliser, hydrogen bond donor |
