1G2O
CRYSTAL STRUCTURE OF PURINE NUCLEOSIDE PHOSPHORYLASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH A TRANSITION-STATE INHIBITOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| A | 0006154 | biological_process | adenosine catabolic process |
| A | 0006161 | biological_process | deoxyguanosine catabolic process |
| A | 0009116 | biological_process | nucleoside metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| B | 0006154 | biological_process | adenosine catabolic process |
| B | 0006161 | biological_process | deoxyguanosine catabolic process |
| B | 0009116 | biological_process | nucleoside metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| C | 0006154 | biological_process | adenosine catabolic process |
| C | 0006161 | biological_process | deoxyguanosine catabolic process |
| C | 0009116 | biological_process | nucleoside metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| 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 | HOH461 |
| A | SER36 |
| A | HIS68 |
| A | ARG88 |
| A | HIS90 |
| A | ASN119 |
| A | ALA120 |
| A | SER208 |
| A | IMH351 |
| 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 | IMH352 |
| B | HOH432 |
| 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 | IMH353 |
| C | HOH510 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IMH A 351 |
| 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 | PO4301 |
| A | HOH501 |
| B | PHE153 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IMH B 352 |
| Chain | Residue |
| B | HIS90 |
| B | TYR92 |
| B | ALA120 |
| B | GLY122 |
| B | TYR188 |
| B | GLU189 |
| B | GLY206 |
| B | MET207 |
| B | ASN231 |
| B | LEU241 |
| B | HIS243 |
| B | PO4302 |
| B | HOH521 |
| C | PHE153 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IMH C 353 |
| Chain | Residue |
| A | PHE153 |
| C | HIS90 |
| C | TYR92 |
| C | ALA120 |
| C | GLY122 |
| C | TYR188 |
| C | GLU189 |
| C | GLY206 |
| C | MET207 |
| C | ASN231 |
| C | LEU241 |
| C | HIS243 |
| C | PO4303 |
| C | HOH420 |
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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11444966","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G2O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1I80","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P45563","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11444966","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ula |
| Chain | Residue | Details |
| A | HIS90 | |
| A | ASN231 | |
| A | GLU93 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ula |
| Chain | Residue | Details |
| B | HIS90 | |
| B | ASN231 | |
| B | GLU93 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ula |
| Chain | Residue | Details |
| C | HIS90 | |
| C | ASN231 | |
| C | GLU93 |
