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 | 0005524 | molecular_function | ATP binding |
A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
A | 0006260 | biological_process | DNA replication |
A | 0008152 | biological_process | metabolic process |
A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
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 | 0005524 | molecular_function | ATP binding |
B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
B | 0006260 | biological_process | DNA replication |
B | 0008152 | biological_process | metabolic process |
B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue TTP A 801 |
Chain | Residue |
A | ASP177 |
A | MG803 |
B | LYS194 |
B | TYR236 |
B | ALA237 |
A | SER178 |
A | LEU179 |
A | ILE182 |
A | ARG207 |
A | ILE213 |
A | LYS214 |
A | THR220 |
A | LYS221 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue ADP A 802 |
Chain | Residue |
A | VAL33 |
A | HIS34 |
A | PHE37 |
A | ASN42 |
A | PHE89 |
A | ARG90 |
A | PHE91 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue MG A 803 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue TTP B 801 |
Chain | Residue |
A | LYS194 |
A | TYR236 |
A | ALA237 |
B | ASP177 |
B | SER178 |
B | LEU179 |
B | ILE182 |
B | ARG207 |
B | ILE213 |
B | LYS214 |
B | THR220 |
B | LYS221 |
B | MG803 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ADP B 802 |
Chain | Residue |
B | HIS34 |
B | PHE37 |
B | ASN42 |
B | ARG90 |
B | PHE91 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue MG B 803 |
Functional Information from PROSITE/UniProt
site_id | PS00089 |
Number of Residues | 23 |
Details | RIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP |
Chain | Residue | Details |
A | TRP558-PRO580 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASN380 | |
A | GLU384 | |
B | ASN380 | |
B | GLU384 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Cysteine radical intermediate => ECO:0000250 |
Chain | Residue | Details |
A | CYS382 | |
B | CYS382 | |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | THR153 | |
B | PRO580 | |
A | SER169 | |
A | GLY198 | |
A | ASN380 | |
A | PRO580 | |
B | THR153 | |
B | SER169 | |
B | GLY198 | |
B | ASN380 | |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for hydrogen atom transfer => ECO:0000250 |
Chain | Residue | Details |
A | CYS170 | |
A | CYS409 | |
B | CYS170 | |
B | CYS409 | |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Allosteric effector binding => ECO:0000250 |
Chain | Residue | Details |
A | ASP177 | |
A | ARG207 | |
B | ASP177 | |
B | ARG207 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Important for electron transfer => ECO:0000250 |
Chain | Residue | Details |
A | TYR683 | |
A | TYR684 | |
B | TYR683 | |
B | TYR684 | |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | SITE: Interacts with thioredoxin/glutaredoxin => ECO:0000250 |
Chain | Residue | Details |
A | CYS695 | |
A | CYS698 | |
B | CYS695 | |
B | CYS698 | |