4COJ
Crystal structure of the anaerobic ribonucleotide reductase from Thermotoga maritima in complex with dATP and CTP
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 | 0006260 | biological_process | DNA replication |
| A | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031250 | cellular_component | anaerobic ribonucleoside-triphosphate reductase complex |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0006260 | biological_process | DNA replication |
| B | 0008998 | molecular_function | ribonucleoside-triphosphate reductase (thioredoxin) activity |
| B | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0031250 | cellular_component | anaerobic ribonucleoside-triphosphate reductase complex |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 652 |
| Chain | Residue |
| A | CYS594 |
| A | HIS598 |
| A | CYS605 |
| A | CYS608 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CTP A 653 |
| Chain | Residue |
| A | ALA173 |
| A | ARG221 |
| A | GLN224 |
| A | TYR227 |
| A | SER358 |
| A | ILE359 |
| A | PRO498 |
| A | ALA499 |
| A | GLU500 |
| A | LYS501 |
| A | ALA502 |
| A | TYR622 |
| A | HOH2012 |
| A | HOH2013 |
| A | HOH2014 |
| A | HOH2015 |
| A | HOH2085 |
| A | TYR112 |
| A | HIS114 |
| A | ASP115 |
| A | TYR124 |
| A | SER171 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DTP A 654 |
| Chain | Residue |
| A | TRP203 |
| A | GLN207 |
| A | GLN210 |
| A | ILE211 |
| A | TYR214 |
| A | SER215 |
| A | GLN218 |
| A | MG655 |
| B | SER146 |
| B | GLU147 |
| B | ALA149 |
| B | LYS150 |
| B | HIS151 |
| B | THR154 |
| B | GLN157 |
| B | HIS158 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 655 |
| Chain | Residue |
| A | GLN207 |
| A | GLN210 |
| A | DTP654 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 652 |
| Chain | Residue |
| B | CYS594 |
| B | HIS598 |
| B | CYS605 |
| B | CYS608 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CTP B 653 |
| Chain | Residue |
| B | TYR112 |
| B | HIS114 |
| B | ASP115 |
| B | TYR124 |
| B | SER171 |
| B | GLY172 |
| B | ALA173 |
| B | ARG221 |
| B | GLN224 |
| B | TYR227 |
| B | SER358 |
| B | ILE359 |
| B | PRO498 |
| B | ALA499 |
| B | GLU500 |
| B | LYS501 |
| B | ALA502 |
| B | TYR622 |
| B | HOH2007 |
| B | HOH2008 |
| B | HOH2009 |
| B | HOH2010 |
| B | HOH2011 |
| B | HOH2014 |
| B | HOH2077 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DTP B 654 |
| Chain | Residue |
| A | SER146 |
| A | GLU147 |
| A | LYS150 |
| A | HIS151 |
| A | THR154 |
| A | GLN157 |
| A | HIS158 |
| A | GLN161 |
| B | TRP203 |
| B | GLN207 |
| B | GLN210 |
| B | ILE211 |
| B | TYR214 |
| B | SER215 |
| B | GLN218 |
| B | MG655 |
| B | HOH2035 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 655 |
| Chain | Residue |
| B | GLN207 |
| B | GLN210 |
| B | DTP654 |
| B | HOH2035 |
