6MYX
EM structure of Bacillus subtilis ribonucleotide reductase inhibited double-helical filament of NrdE alpha subunit with dATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| I | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| I | 0005524 | molecular_function | ATP binding |
| I | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| I | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| I | 0016491 | molecular_function | oxidoreductase activity |
| J | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| J | 0005524 | molecular_function | ATP binding |
| J | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| J | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue DTP C 1001 |
| Chain | Residue |
| C | ASP177 |
| D | TYR236 |
| C | SER178 |
| C | LEU179 |
| C | ILE182 |
| C | ARG207 |
| C | ILE213 |
| C | LYS214 |
| C | HIS304 |
| D | LYS194 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue DTP C 1002 |
| Chain | Residue |
| C | VAL33 |
| C | HIS34 |
| C | PHE37 |
| C | ASN42 |
| C | PHE89 |
| C | ARG90 |
| C | PHE91 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue DTP D 1001 |
| Chain | Residue |
| C | LYS194 |
| C | TYR236 |
| D | ASP177 |
| D | SER178 |
| D | LEU179 |
| D | ILE182 |
| D | ARG207 |
| D | ILE213 |
| D | LYS214 |
| D | HIS304 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue DTP D 1002 |
| Chain | Residue |
| D | VAL33 |
| D | HIS34 |
| D | PHE37 |
| D | ASN42 |
| D | PHE89 |
| D | ARG90 |
| D | PHE91 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue DTP I 1001 |
| Chain | Residue |
| I | ASP177 |
| I | SER178 |
| I | LEU179 |
| I | ILE182 |
| I | ARG207 |
| I | ILE213 |
| I | LYS214 |
| I | HIS304 |
| J | LYS194 |
| J | TYR236 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue DTP I 1002 |
| Chain | Residue |
| I | VAL33 |
| I | HIS34 |
| I | PHE37 |
| I | ASN42 |
| I | PHE89 |
| I | ARG90 |
| I | PHE91 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue DTP J 1001 |
| Chain | Residue |
| I | LYS194 |
| I | TYR236 |
| J | ASP177 |
| J | SER178 |
| J | LEU179 |
| J | ILE182 |
| J | ARG207 |
| J | ILE213 |
| J | LYS214 |
| J | HIS304 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue DTP J 1002 |
| Chain | Residue |
| J | VAL33 |
| J | HIS34 |
| J | PHE37 |
| J | ASN42 |
| J | PHE89 |
| J | ARG90 |
| J | PHE91 |
Functional Information from PROSITE/UniProt
| site_id | PS00089 |
| Number of Residues | 23 |
| Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP |
| Chain | Residue | Details |
| C | TRP558-PRO580 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| C | ASN380 | |
| C | GLU384 | |
| D | ASN380 | |
| D | GLU384 | |
| I | ASN380 | |
| I | GLU384 | |
| J | ASN380 | |
| J | GLU384 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Cysteine radical intermediate => ECO:0000250 |
| Chain | Residue | Details |
| C | CYS382 | |
| D | CYS382 | |
| I | CYS382 | |
| J | CYS382 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| C | PRO580 | |
| D | THR153 | |
| D | SER169 | |
| D | GLY198 | |
| D | ASN380 | |
| D | PRO580 | |
| I | THR153 | |
| I | SER169 | |
| I | GLY198 | |
| I | ASN380 | |
| I | PRO580 | |
| J | THR153 | |
| J | SER169 | |
| J | GLY198 | |
| J | ASN380 | |
| J | PRO580 | |
| C | THR153 | |
| C | SER169 | |
| C | GLY198 | |
| C | ASN380 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Important for hydrogen atom transfer => ECO:0000250 |
| Chain | Residue | Details |
| I | CYS170 | |
| I | CYS409 | |
| J | CYS170 | |
| J | CYS409 | |
| C | CYS170 | |
| C | CYS409 | |
| D | CYS170 | |
| D | CYS409 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Allosteric effector binding => ECO:0000250 |
| Chain | Residue | Details |
| C | ASP177 | |
| C | ARG207 | |
| D | ASP177 | |
| D | ARG207 | |
| I | ASP177 | |
| I | ARG207 | |
| J | ASP177 | |
| J | ARG207 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Important for electron transfer => ECO:0000250 |
| Chain | Residue | Details |
| C | TYR683 | |
| C | TYR684 | |
| D | TYR683 | |
| D | TYR684 | |
| I | TYR683 | |
| I | TYR684 | |
| J | TYR683 | |
| J | TYR684 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | SITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250 |
| Chain | Residue | Details |
| C | CYS695 | |
| C | CYS698 | |
| D | CYS695 | |
| D | CYS698 | |
| I | CYS695 | |
| I | CYS698 | |
| J | CYS695 | |
| J | CYS698 |
