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 | THR153 | |
D | PRO580 | |
I | THR153 | |
I | SER169 | |
I | GLY198 | |
I | ASN380 | |
I | PRO580 | |
J | THR153 | |
J | SER169 | |
J | GLY198 | |
J | ASN380 | |
C | SER169 | |
J | PRO580 | |
C | GLY198 | |
C | ASN380 | |
C | PRO580 | |
D | THR153 | |
D | SER169 | |
D | GLY198 | |
D | ASN380 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Important for hydrogen atom transfer => ECO:0000250 |
Chain | Residue | Details |
C | CYS170 | |
C | CYS409 | |
D | CYS170 | |
D | CYS409 | |
I | CYS170 | |
I | CYS409 | |
J | CYS170 | |
J | 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 |