2BQ1
Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| E | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| F | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| I | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| I | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| I | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| J | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| J | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG E 1701 |
| Chain | Residue |
| E | DGT1700 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG F 1701 |
| Chain | Residue |
| F | DGT1700 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE I 1320 |
| Chain | Residue |
| I | ASP67 |
| I | GLU98 |
| I | HIS101 |
| I | PHE162 |
| I | GLU192 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE I 1321 |
| Chain | Residue |
| I | GLU192 |
| I | HIS195 |
| I | GLU98 |
| I | GLU158 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE J 1287 |
| Chain | Residue |
| J | ASP67 |
| J | GLU98 |
| J | HIS101 |
| J | GLU192 |
| J | FE1288 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE J 1288 |
| Chain | Residue |
| J | GLU98 |
| J | GLU158 |
| J | GLU192 |
| J | HIS195 |
| J | FE1287 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DGT E 1700 |
| Chain | Residue |
| E | ASP185 |
| E | ASN186 |
| E | MET187 |
| E | ILE190 |
| E | ARG215 |
| E | ILE221 |
| E | LYS222 |
| E | MG1701 |
| F | LYS202 |
| F | TYR244 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DGT F 1700 |
| Chain | Residue |
| E | LYS202 |
| E | TYR244 |
| F | ASP185 |
| F | ASN186 |
| F | MET187 |
| F | ARG215 |
| F | ILE221 |
| F | LYS222 |
| F | MG1701 |
Functional Information from PROSITE/UniProt
| site_id | PS00089 |
| Number of Residues | 23 |
| Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WlkLrddvmryGIYNqnlQAvpP |
| Chain | Residue | Details |
| E | TRP566-PRO588 |
| site_id | PS00368 |
| Number of Residues | 17 |
| Details | RIBORED_SMALL Ribonucleotide reductase small subunit signature. MEa.VHArSYssIfstLC |
| Chain | Residue | Details |
| I | MET97-CYS113 |
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 | 22 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Allosteric effector binding"} |
| 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 | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10014","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| I | TYR105 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| J | TYR105 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| E | CYS388 | |
| E | CYS415 | |
| E | ASN386 | |
| E | GLU390 | |
| E | CYS178 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| F | CYS388 | |
| F | CYS415 | |
| F | ASN386 | |
| F | GLU390 | |
| F | CYS178 |
