1YFD
Crystal structure of the Y122H mutant of ribonucleotide reductase R2 protein from E. 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 | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 601 |
| Chain | Residue |
| A | TYR157 |
| A | CYS196 |
| A | VAL200 |
| A | HOH623 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 602 |
| Chain | Residue |
| B | TYR157 |
| B | CYS196 |
| B | VAL200 |
| B | HG604 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG B 603 |
| Chain | Residue |
| B | ALA265 |
| B | CYS268 |
| B | LYS269 |
| B | HG613 |
| B | HOH752 |
| B | TYR194 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG B 604 |
| Chain | Residue |
| B | TYR156 |
| B | TYR157 |
| B | CYS196 |
| B | VAL200 |
| B | HG602 |
| B | HOH637 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 605 |
| Chain | Residue |
| A | TYR194 |
| A | ALA265 |
| A | CYS272 |
| A | HOH766 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG A 606 |
| Chain | Residue |
| A | VAL210 |
| A | CYS214 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 607 |
| Chain | Residue |
| B | ASN76 |
| B | CYS214 |
| B | LEU290 |
| B | LEU304 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 608 |
| Chain | Residue |
| B | MET198 |
| B | CYS272 |
| B | LEU275 |
| B | PHE276 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE HG A 609 |
| Chain | Residue |
| A | CYS305 |
| A | GLU309 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG B 610 |
| Chain | Residue |
| B | CYS305 |
| B | GLN306 |
| B | GLU309 |
| B | HG611 |
| B | HOH794 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 611 |
| Chain | Residue |
| B | LYS284 |
| B | CYS305 |
| B | GLU309 |
| B | HG610 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG B 612 |
| Chain | Residue |
| B | LYS191 |
| B | ILE264 |
| B | GLU267 |
| B | CYS268 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE HG B 613 |
| Chain | Residue |
| B | TYR194 |
| B | ALA265 |
| B | HG603 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FEO A 501 |
| Chain | Residue |
| A | ASP84 |
| A | GLU115 |
| A | HIS118 |
| A | GLU204 |
| A | GLU238 |
| A | HIS241 |
| A | HOH610 |
| A | HOH611 |
| A | HOH612 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FEO B 502 |
| Chain | Residue |
| B | ASP84 |
| B | GLU115 |
| B | HIS118 |
| B | GLU204 |
| B | GLU238 |
| B | HIS241 |
| B | HOH614 |
| B | HOH615 |
| B | HOH616 |
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 | HIS122 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xik |
| Chain | Residue | Details |
| B | HIS122 |
| 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 |
