3HNF
Crystal structure of human ribonucleotide reductase 1 bound to the effectors TTP and dATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000731 | biological_process | DNA synthesis involved in DNA repair |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0006264 | biological_process | mitochondrial DNA replication |
| A | 0006281 | biological_process | DNA repair |
| A | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0010971 | biological_process | positive regulation of G2/M transition of mitotic cell cycle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0017076 | molecular_function | purine nucleotide binding |
| A | 0036175 | molecular_function | ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051290 | biological_process | protein heterotetramerization |
| A | 0061731 | molecular_function | ribonucleoside-diphosphate reductase activity |
| A | 0070318 | biological_process | positive regulation of G0 to G1 transition |
| A | 0097718 | molecular_function | disordered domain specific binding |
| A | 1900087 | biological_process | positive regulation of G1/S transition of mitotic cell cycle |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000731 | biological_process | DNA synthesis involved in DNA repair |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0006264 | biological_process | mitochondrial DNA replication |
| B | 0006281 | biological_process | DNA repair |
| B | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| B | 0010971 | biological_process | positive regulation of G2/M transition of mitotic cell cycle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0017076 | molecular_function | purine nucleotide binding |
| B | 0036175 | molecular_function | ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051290 | biological_process | protein heterotetramerization |
| B | 0061731 | molecular_function | ribonucleoside-diphosphate reductase activity |
| B | 0070318 | biological_process | positive regulation of G0 to G1 transition |
| B | 0097718 | molecular_function | disordered domain specific binding |
| B | 1900087 | biological_process | positive regulation of G1/S transition of mitotic cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | TTP804 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TTP A 804 |
| Chain | Residue |
| A | MG801 |
| B | LYS243 |
| B | ASP287 |
| A | ASP226 |
| A | SER227 |
| A | ILE228 |
| A | ARG256 |
| A | ILE262 |
| A | ALA263 |
| A | GLY264 |
| A | THR265 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 807 |
| Chain | Residue |
| A | SER202 |
| A | THR604 |
| A | ALA605 |
| A | SER606 |
| A | THR607 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 808 |
| Chain | Residue |
| A | ILE136 |
| A | TYR137 |
| A | ASP138 |
| B | LYS382 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 802 |
| Chain | Residue |
| B | ASP226 |
| B | TTP803 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TTP B 803 |
| Chain | Residue |
| A | LYS243 |
| A | VAL286 |
| A | ASP287 |
| B | ASP226 |
| B | SER227 |
| B | ILE228 |
| B | ARG256 |
| B | ILE262 |
| B | ALA263 |
| B | GLY264 |
| B | THR265 |
| B | MG802 |
| B | HOH822 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DTP B 805 |
| Chain | Residue |
| B | LYS5 |
| B | ARG6 |
| B | ARG12 |
| B | MET14 |
| B | ILE18 |
| B | ARG21 |
| B | THR53 |
| B | LEU56 |
| B | LYS88 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 806 |
| Chain | Residue |
| B | SER202 |
| B | PRO603 |
| B | THR604 |
| B | ALA605 |
| B | SER606 |
| B | THR607 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 809 |
| Chain | Residue |
| B | SER687 |
| B | GLN688 |
| B | LYS689 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3HNE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3HND","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 91 |
| Details | Domain: {"description":"ATP-cone","evidences":[{"source":"PROSITE-ProRule","id":"PRU00492","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
