2AV8
Y122F MUTANT OF RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| A | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004748 | molecular_function | ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0009185 | biological_process | ribonucleoside diphosphate metabolic process |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0009265 | biological_process | 2'-deoxyribonucleotide biosynthetic process |
| B | 0015949 | biological_process | nucleobase-containing small molecule interconversion |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 402 |
| Chain | Residue |
| A | GLU69 |
| A | ARG221 |
| A | HOH1243 |
| A | HOH1276 |
| A | HOH1338 |
| B | GLU69 |
| B | ARG221 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO A 401 |
| Chain | Residue |
| A | HIS118 |
| A | GLU204 |
| A | GLU238 |
| A | HIS241 |
| A | HOH1201 |
| A | HOH1202 |
| A | ASP84 |
| A | GLU115 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FEO B 403 |
| Chain | Residue |
| B | ASP84 |
| B | GLU115 |
| B | HIS118 |
| B | GLU204 |
| B | GLU238 |
| B | HIS241 |
| B | HOH1203 |
| B | HOH1204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | THR123 | |
| B | THR123 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER85 | |
| B | ALA205 | |
| B | ALA239 | |
| B | LEU242 | |
| A | THR116 | |
| A | SER119 | |
| A | ALA205 | |
| A | ALA239 | |
| A | LEU242 | |
| B | SER85 | |
| B | THR116 | |
| B | SER119 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| A | PHE122 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| B | PHE122 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 918 |
| Chain | Residue | Details |
| A | THR123 | pi-pi interaction, single electron relay |
| A | GLU238 |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 918 |
| Chain | Residue | Details |
| B | THR123 | pi-pi interaction, single electron relay |
| B | GLU238 |
