3PAW
Low resolution X-ray crystal structure of Yeast Rnr1p with dATP bound in the A-site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS00089 |
| Number of Residues | 23 |
| Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WdtLrkdimkhGVRNsltMApmP |
| Chain | Residue | Details |
| A | TRP585-PRO607 |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ISQkTIINMAADRSVyI |
| Chain | Residue | Details |
| A | ILE690-ILE706 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | ASN426 | |
| A | GLU430 | |
| B | ASN426 | |
| B | GLU430 | |
| C | ASN426 | |
| C | GLU430 | |
| D | ASN426 | |
| D | GLU430 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Cysteine radical intermediate |
| Chain | Residue | Details |
| A | CYS428 | |
| B | CYS428 | |
| C | CYS428 | |
| D | CYS428 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 52 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P23921 |
| Chain | Residue | Details |
| A | LYS5 | |
| A | ALA263 | |
| A | ASN426 | |
| A | GLU430 | |
| A | THR608 | |
| B | LYS5 | |
| B | GLU11 | |
| B | THR53 | |
| B | ASP57 | |
| B | SER202 | |
| B | SER217 | |
| A | GLU11 | |
| B | ASP226 | |
| B | LYS243 | |
| B | ARG256 | |
| B | ALA263 | |
| B | ASN426 | |
| B | GLU430 | |
| B | THR608 | |
| C | LYS5 | |
| C | GLU11 | |
| C | THR53 | |
| A | THR53 | |
| C | ASP57 | |
| C | SER202 | |
| C | SER217 | |
| C | ASP226 | |
| C | LYS243 | |
| C | ARG256 | |
| C | ALA263 | |
| C | ASN426 | |
| C | GLU430 | |
| C | THR608 | |
| A | ASP57 | |
| D | LYS5 | |
| D | GLU11 | |
| D | THR53 | |
| D | ASP57 | |
| D | SER202 | |
| D | SER217 | |
| D | ASP226 | |
| D | LYS243 | |
| D | ARG256 | |
| D | ALA263 | |
| A | SER202 | |
| D | ASN426 | |
| D | GLU430 | |
| D | THR608 | |
| A | SER217 | |
| A | ASP226 | |
| A | LYS243 | |
| A | ARG256 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Important for hydrogen atom transfer => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS218 | |
| A | CYS443 | |
| B | CYS218 | |
| B | CYS443 | |
| C | CYS218 | |
| C | CYS443 | |
| D | CYS218 | |
| D | CYS443 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Important for electron transfer => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR741 | |
| A | TYR742 | |
| B | TYR741 | |
| B | TYR742 | |
| C | TYR741 | |
| C | TYR742 | |
| D | TYR741 | |
| D | TYR742 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS883 | |
| A | CYS886 | |
| B | CYS883 | |
| B | CYS886 | |
| C | CYS883 | |
| C | CYS886 | |
| D | CYS883 | |
| D | CYS886 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER227 | |
| A | SER837 | |
| B | SER227 | |
| B | SER837 | |
| C | SER227 | |
| C | SER837 | |
| D | SER227 | |
| D | SER837 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21672 |
| Chain | Residue | Details |
| A | SER816 | |
| B | SER816 | |
| C | SER816 | |
| D | SER816 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER887 | |
| B | SER887 | |
| C | SER887 | |
| D | SER887 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
| Chain | Residue | Details |
| A | LYS387 | |
| D | LYS387 | |
| D | LYS853 | |
| A | LYS853 | |
| B | LYS387 | |
| B | LYS853 | |
| C | LYS387 | |
| C | LYS853 |
