Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1743 |
| Chain | Residue |
| A | ALA447 |
| A | SER448 |
| A | MET602 |
| A | THR604 |
| A | SER606 |
| A | THR607 |
| A | HOH2019 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1744 |
| Chain | Residue |
| A | HOH2115 |
| A | HOH2118 |
| A | DTP1745 |
| A | HOH2114 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE DTP A 1745 |
| Chain | Residue |
| A | ASP226 |
| A | SER227 |
| A | ILE228 |
| A | ARG256 |
| A | ILE262 |
| A | ALA263 |
| A | GLY264 |
| A | MG1744 |
| A | HOH2026 |
| A | HOH2114 |
| A | HOH2115 |
| A | HOH2116 |
| A | HOH2117 |
| A | HOH2118 |
| B | LYS243 |
| B | TYR285 |
| B | VAL286 |
| B | ASP287 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DTP B 1745 |
| Chain | Residue |
| A | LYS243 |
| A | TYR285 |
| A | VAL286 |
| A | ASP287 |
| B | ASP226 |
| B | SER227 |
| B | ILE228 |
| B | ARG256 |
| B | ILE262 |
| B | ALA263 |
| B | GLY264 |
| B | MG1746 |
| B | HOH2109 |
| B | HOH2110 |
| B | HOH2111 |
| B | HOH2112 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1746 |
| Chain | Residue |
| B | DTP1745 |
| B | HOH2110 |
| B | HOH2111 |
| B | HOH2112 |
Functional Information from PROSITE/UniProt
| site_id | PS00089 |
| Number of Residues | 23 |
| Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WkvLkekiakyGIRNsllIApmP |
| Chain | Residue | Details |
| A | TRP581-PRO603 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3HND","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3HNE","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3r1r |
| Chain | Residue | Details |
| A | GLU431 | |
| A | CYS218 | |
| A | CYS429 | |
| A | CYS444 | |
| A | ASN427 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3r1r |
| Chain | Residue | Details |
| B | GLU431 | |
| B | CYS218 | |
| B | CYS429 | |
| B | CYS444 | |
| B | ASN427 | |
2WGH
