7MMQ
Crystal Structure of the Class Ie Ribonucleotide Reductase Beta-NrdI complex from Aerococcus urinae in Reduced Hydroquinone Form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| A | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| B | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| C | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0005971 | cellular_component | ribonucleoside-diphosphate reductase complex |
| D | 0009263 | biological_process | deoxyribonucleotide biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0010181 | molecular_function | FMN binding |
| E | 0036211 | biological_process | protein modification process |
| F | 0010181 | molecular_function | FMN binding |
| F | 0036211 | biological_process | protein modification process |
| G | 0010181 | molecular_function | FMN binding |
| G | 0036211 | biological_process | protein modification process |
| H | 0010181 | molecular_function | FMN binding |
| H | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | TYR6 |
| B | SER11 |
| B | ARG25 |
| B | SER100 |
| B | LEU101 |
| B | GLN106 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 401 |
| Chain | Residue |
| C | ARG25 |
| C | SER100 |
| C | LEU101 |
| C | GLN106 |
| C | TYR6 |
| C | SER11 |
| C | GLU14 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 401 |
| Chain | Residue |
| D | TYR6 |
| D | SER11 |
| D | GLU14 |
| D | ARG25 |
| D | SER100 |
| D | LEU101 |
| D | GLU103 |
| D | GLN106 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue FMN E 201 |
| Chain | Residue |
| A | PHE215 |
| E | SER9 |
| E | THR10 |
| E | SER12 |
| E | ASN13 |
| E | ASN14 |
| E | THR15 |
| E | PRO48 |
| E | THR49 |
| E | TYR50 |
| E | SER51 |
| E | GLY91 |
| E | ASN92 |
| E | PHE95 |
| E | SER98 |
| E | PHE99 |
| E | ALA100 |
| E | LEU120 |
| E | HOH301 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | binding site for residue FMN G 201 |
| Chain | Residue |
| C | ARG43 |
| G | SER9 |
| G | THR10 |
| G | SER12 |
| G | ASN13 |
| G | ASN14 |
| G | THR15 |
| G | PRO48 |
| G | THR49 |
| G | TYR50 |
| G | SER51 |
| G | GLY91 |
| G | ASN92 |
| G | PHE95 |
| G | SER98 |
| G | PHE99 |
| G | ALA100 |
| G | LEU120 |
| G | HOH303 |
| G | HOH305 |
| G | HOH306 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue FMN F 201 |
| Chain | Residue |
| F | SER9 |
| F | THR10 |
| F | SER12 |
| F | ASN13 |
| F | ASN14 |
| F | THR15 |
| F | PRO48 |
| F | THR49 |
| F | TYR50 |
| F | SER51 |
| F | GLY91 |
| F | ASN92 |
| F | PHE95 |
| F | SER98 |
| F | PHE99 |
| F | ALA100 |
| F | LEU120 |
| F | HOH303 |
| F | HOH304 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for residue FMN H 201 |
| Chain | Residue |
| D | ARG43 |
| H | SER9 |
| H | THR10 |
| H | SER12 |
| H | ASN13 |
| H | ASN14 |
| H | THR15 |
| H | PRO48 |
| H | THR49 |
| H | TYR50 |
| H | SER51 |
| H | GLY91 |
| H | ASN92 |
| H | PHE95 |
| H | SER98 |
| H | PHE99 |
| H | ALA100 |
| H | LEU120 |
| H | HOH302 |






