1XJF
Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG B 1003 |
Chain | Residue |
B | DTP1001 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG A 1004 |
Chain | Residue |
A | DTP1002 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE DTP B 1001 |
Chain | Residue |
B | ARG171 |
B | VAL177 |
B | ALA178 |
B | GLY179 |
B | THR180 |
B | LYS183 |
B | ALA184 |
B | SER185 |
B | PHE190 |
B | MG1003 |
B | HOH1005 |
A | LYS158 |
A | VAL200 |
A | LYS202 |
B | ASP141 |
B | SER142 |
B | ILE143 |
B | ILE146 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE DTP A 1002 |
Chain | Residue |
A | ASP141 |
A | SER142 |
A | ILE143 |
A | ILE146 |
A | ARG171 |
A | VAL177 |
A | ALA178 |
A | GLY179 |
A | THR180 |
A | LYS183 |
A | ALA184 |
A | SER185 |
A | PHE190 |
A | MG1004 |
A | HOH1026 |
B | LYS158 |
B | VAL200 |
B | VAL201 |
B | LYS202 |