1XJN
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-CDP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0031419 | molecular_function | cobalamin binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0031419 | molecular_function | cobalamin binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0031419 | molecular_function | cobalamin binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| D | 0005524 | molecular_function | ATP binding |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0031419 | molecular_function | cobalamin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1009 |
| Chain | Residue |
| B | SER91 |
| B | ARG207 |
| B | CDP1001 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE CDP B 1001 |
| Chain | Residue |
| B | ARG208 |
| B | ASN320 |
| B | PRO321 |
| B | CYS322 |
| B | GLU324 |
| B | ALA489 |
| B | PRO490 |
| B | THR491 |
| B | GLY492 |
| B | SER493 |
| B | ILE494 |
| B | CL1009 |
| B | HOH1027 |
| B | HOH1101 |
| B | HOH1119 |
| B | ASN90 |
| B | SER91 |
| B | ALA133 |
| B | GLY162 |
| B | GLN203 |
| B | ARG207 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CDP A 1002 |
| Chain | Residue |
| A | ASN90 |
| A | SER91 |
| A | ALA133 |
| A | GLY162 |
| A | GLN203 |
| A | ALA210 |
| A | ASN320 |
| A | PRO321 |
| A | CYS322 |
| A | GLU324 |
| A | ALA489 |
| A | PRO490 |
| A | THR491 |
| A | GLY492 |
| A | SER493 |
| A | ILE494 |
| A | HOH1051 |
| A | HOH1184 |
| A | HOH1185 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CDP D 1003 |
| Chain | Residue |
| D | ASN90 |
| D | SER91 |
| D | ALA133 |
| D | GLY162 |
| D | ASN320 |
| D | PRO321 |
| D | CYS322 |
| D | GLU324 |
| D | ALA489 |
| D | PRO490 |
| D | THR491 |
| D | GLY492 |
| D | SER493 |
| D | ILE494 |
| D | HOH1066 |
| D | HOH1108 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE CDP C 1004 |
| Chain | Residue |
| C | ASN90 |
| C | SER91 |
| C | ALA133 |
| C | GLY161 |
| C | GLY162 |
| C | ALA210 |
| C | ASN320 |
| C | PRO321 |
| C | CYS322 |
| C | GLU324 |
| C | ALA489 |
| C | PRO490 |
| C | THR491 |
| C | GLY492 |
| C | SER493 |
| C | ILE494 |
| C | HOH1091 |
| C | HOH1131 |
| C | HOH1172 |
| C | HOH1173 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DTP A 1005 |
| Chain | Residue |
| A | ASP141 |
| A | SER142 |
| A | ILE143 |
| A | ARG171 |
| A | VAL177 |
| A | ALA178 |
| A | SER185 |
| A | HOH1067 |
| A | HOH1082 |
| A | HOH1089 |
| B | LYS158 |
| B | VAL200 |
| B | VAL201 |
| B | LYS202 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DTP B 1006 |
| Chain | Residue |
| B | ILE143 |
| B | ARG171 |
| B | VAL177 |
| B | LYS183 |
| B | ALA184 |
| B | SER185 |
| B | PHE190 |
| B | HOH1075 |
| B | HOH1109 |
| B | HOH1129 |
| B | HOH1134 |
| A | HIS127 |
| A | LYS158 |
| A | VAL200 |
| A | LYS202 |
| B | ASP141 |
| B | SER142 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DTP C 1007 |
| Chain | Residue |
| C | ASP141 |
| C | SER142 |
| C | ILE143 |
| C | ILE146 |
| C | ARG171 |
| C | VAL177 |
| C | LYS183 |
| C | SER185 |
| D | LYS158 |
| D | VAL200 |
| D | LYS202 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE DTP C 1008 |
| Chain | Residue |
| C | HIS127 |
| C | LYS158 |
| C | VAL200 |
| C | VAL201 |
| C | LYS202 |
| C | GLN203 |
| C | HOH1119 |
| C | HOH1121 |
| C | HOH1155 |
| C | HOH1175 |
| D | ASP141 |
| D | SER142 |
| D | ILE143 |
| D | ARG171 |
| D | VAL177 |
| D | ALA178 |
| D | LYS183 |
| D | ALA184 |
| D | SER185 |
| D | HOH1013 |
