2BQ1
Ribonucleotide reductase class 1b holocomplex R1E,R2F from Salmonella typhimurium
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10014 |
Chain | Residue | Details |
I | TYR105 | |
J | TYR105 | |
F | LEU387 | |
F | ILE391 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
I | ASP67 | |
J | GLU158 | |
J | GLU192 | |
J | HIS195 | |
I | GLU98 | |
I | HIS101 | |
I | GLU158 | |
I | GLU192 | |
I | HIS195 | |
J | ASP67 | |
J | GLU98 | |
J | HIS101 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
E | PRO162 | |
F | THR589 | |
E | CYS178 | |
E | VAL207 | |
E | LEU387 | |
E | THR589 | |
F | PRO162 | |
F | CYS178 | |
F | VAL207 | |
F | LEU387 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for hydrogen atom transfer => ECO:0000250 |
Chain | Residue | Details |
E | PHE179 | |
E | ASN416 | |
F | PHE179 | |
F | ASN416 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | SITE: Allosteric effector binding |
Chain | Residue | Details |
E | ASN186 | |
E | GLU216 | |
E | ARG223 | |
F | ASN186 | |
F | GLU216 | |
F | ARG223 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Important for electron transfer => ECO:0000250 |
Chain | Residue | Details |
E | TYR693 | |
E | ILE694 | |
F | TYR693 | |
F | ILE694 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | SITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250 |
Chain | Residue | Details |
E | VAL710 | |
E | ALA713 | |
F | VAL710 | |
F | ALA713 |
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 |