1BRW
THE CRYSTAL STRUCTURE OF PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE IN A CLOSED CONFORMATION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0004850 | molecular_function | uridine phosphorylase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| A | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| A | 0009032 | molecular_function | thymidine phosphorylase activity |
| A | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
| B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| B | 0004850 | molecular_function | uridine phosphorylase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006206 | biological_process | pyrimidine nucleobase metabolic process |
| B | 0006213 | biological_process | pyrimidine nucleoside metabolic process |
| B | 0009032 | molecular_function | thymidine phosphorylase activity |
| B | 0016154 | molecular_function | pyrimidine-nucleoside phosphorylase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047847 | molecular_function | deoxyuridine phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | ACTIVE SITE |
| Chain | Residue |
| A | LYS187 |
| A | SER83 |
| A | ARG168 |
| A | TYR165 |
| A | SER183 |
| A | SER182 |
| A | SER110 |
| A | LYS108 |
| A | THR120 |
| A | LYS81 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | ACTIVE SITE |
| Chain | Residue |
| B | LYS1187 |
| B | ARG1168 |
| B | TYR1165 |
| B | SER1183 |
| B | SER1182 |
| B | SER1110 |
| B | LYS1108 |
| B | THR1120 |
| B | LYS1081 |
| B | SER1083 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
| Chain | Residue |
| A | LYS81 |
| A | HIS82 |
| A | SER83 |
| A | THR92 |
| A | LYS108 |
| A | SER110 |
| A | THR120 |
| A | HOH4003 |
| A | HOH4012 |
| A | HOH4105 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2002 |
| Chain | Residue |
| B | LYS1081 |
| B | HIS1082 |
| B | SER1083 |
| B | THR1092 |
| B | LYS1108 |
| B | SER1110 |
| B | THR1120 |
| B | HOH4066 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 3001 |
| Chain | Residue |
| A | GLY88 |
| A | THR90 |
| A | LEU243 |
| A | ALA246 |
| A | GLU255 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 3002 |
| Chain | Residue |
| B | GLY1088 |
| B | THR1090 |
| B | LEU1243 |
| B | ALA1246 |
| B | GLU1255 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE URA B 5001 |
| Chain | Residue |
| B | HIS1082 |
| B | SER1083 |
| B | THR1084 |
| B | LEU1114 |
| B | TYR1165 |
| B | ARG1168 |
| B | ILE1180 |
| B | SER1183 |
| B | ILE1184 |
| B | LYS1187 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MES B 6001 |
| Chain | Residue |
| B | LYS1018 |
| B | GLU1022 |
| B | ARG1026 |
| B | GLN1064 |
| B | HOH4019 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 6002 |
| Chain | Residue |
| A | TYR46 |
| A | ARG48 |
| A | GLY49 |
| A | ARG216 |
| A | HOH4021 |
| A | HOH4071 |
Functional Information from PROSITE/UniProt
| site_id | PS00647 |
| Number of Residues | 16 |
| Details | THYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTiDkLE |
| Chain | Residue | Details |
| A | SER110-GLU125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9817849","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BRW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9817849 |
| Chain | Residue | Details |
| A | LYS187 | |
| A | SER183 | |
| A | HIS82 | |
| A | ARG168 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9817849 |
| Chain | Residue | Details |
| B | SER1183 | |
| B | ARG1168 | |
| B | HIS1082 | |
| B | LYS1187 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 91 |
| Chain | Residue | Details |
| A | HIS82 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP161 | electrostatic stabiliser |
| A | ARG168 | electrostatic stabiliser, hydrogen bond donor |
| A | SER183 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS187 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 91 |
| Chain | Residue | Details |
| B | HIS1082 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP1161 | electrostatic stabiliser |
| B | ARG1168 | electrostatic stabiliser, hydrogen bond donor |
| B | SER1183 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS1187 | electrostatic stabiliser, hydrogen bond donor |
