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 | 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 | 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 | 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 | 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 | 22 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9817849, ECO:0007744|PDB:1BRW |
Chain | Residue | Details |
A | LYS81 | |
A | ALA246 | |
A | GLU255 | |
B | LYS1081 | |
B | GLY1088 | |
B | THR1090 | |
B | THR1092 | |
B | LYS1108 | |
B | THR1120 | |
B | ARG1168 | |
B | LYS1187 | |
A | GLY88 | |
B | LEU1243 | |
B | ALA1246 | |
B | GLU1255 | |
A | THR90 | |
A | THR92 | |
A | LYS108 | |
A | THR120 | |
A | ARG168 | |
A | LYS187 | |
A | LEU243 |
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 |