6EBZ
Crystal Structure of the Class Ie Ribonucleotide Reductase Beta Subunit from Aerococcus urinae in Activated Form with Thiocyanate Bound
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | GLY263 |
| A | GLU267 |
| A | HOH623 |
| B | GLY261 |
| B | HOH639 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| B | LEU264 |
| B | ALA265 |
| B | HOH612 |
| A | ASP260 |
| B | HIS256 |
| B | TYR259 |
| B | ASP260 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue SCN B 401 |
| Chain | Residue |
| B | PHE241 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SCN B 402 |
| Chain | Residue |
| B | LEU84 |
| B | ASP85 |
| B | GLN88 |
| B | MET175 |
| B | PRO176 |
| B | LEU180 |
| B | LYS210 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SCN B 403 |
| Chain | Residue |
| A | GLU137 |
| B | TYR5 |
| B | ASN28 |
| B | LYS31 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 404 |
| Chain | Residue |
| B | SER128 |
| B | HOH551 |
| B | HOH582 |
| B | HOH585 |
| B | HOH666 |
| C | HOH545 |
| C | HOH557 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 405 |
| Chain | Residue |
| A | GLY261 |
| A | HOH648 |
| B | GLY263 |
| B | GLU267 |
| B | HOH591 |
| B | HOH628 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | ASP68 |
| B | ASP69 |
| C | LYS232 |
| C | GLU235 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SCN C 401 |
| Chain | Residue |
| C | PHE241 |
| C | HOH624 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SCN C 402 |
| Chain | Residue |
| C | ASP260 |
| C | GLY263 |
| C | ALA265 |
| C | ASP266 |
| C | GLU267 |
| C | CA404 |
| D | ASP260 |
| D | GLY261 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 403 |
| Chain | Residue |
| B | HOH560 |
| B | HOH592 |
| C | SER128 |
| C | HOH561 |
| C | HOH587 |
| C | HOH648 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 404 |
| Chain | Residue |
| C | GLY263 |
| C | GLU267 |
| C | SCN402 |
| C | HOH601 |
| D | GLY261 |
| D | HOH620 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 401 |
| Chain | Residue |
| C | GLY261 |
| D | GLY263 |
| D | ASP266 |
| D | GLU267 |
| D | HOH607 |
| D | HOH621 |
| site_id | AD5 |
| Number of Residues | 15 |
| Details | binding site for Ligand residues DAH A 123 through GLY A 124 bound to SER A 122 |
| Chain | Residue |
| A | PHE78 |
| A | LEU81 |
| A | THR82 |
| A | ASP85 |
| A | HIS119 |
| A | ALA120 |
| A | ARG121 |
| A | SER122 |
| A | THR125 |
| A | ILE126 |
| A | PHE127 |
| A | SER128 |
| A | PHE184 |
| A | ILE206 |
| B | ASN30 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for Ligand residues DAH B 123 through GLY B 124 bound to SER B 122 |
| Chain | Residue |
| A | ASN30 |
| B | LEU81 |
| B | THR82 |
| B | ASP85 |
| B | HIS119 |
| B | ALA120 |
| B | ARG121 |
| B | SER122 |
| B | THR125 |
| B | ILE126 |
| B | PHE127 |
| B | SER128 |
| B | PHE184 |
| B | HOH515 |
| B | HOH558 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for Ligand residues DAH C 123 through GLY C 124 bound to SER C 122 |
| Chain | Residue |
| C | LEU81 |
| C | THR82 |
| C | ASP85 |
| C | HIS119 |
| C | ALA120 |
| C | ARG121 |
| C | SER122 |
| C | THR125 |
| C | ILE126 |
| C | PHE127 |
| C | SER128 |
| C | PHE184 |
| C | ILE206 |
| C | HOH501 |
| D | ASN30 |
| site_id | AD8 |
| Number of Residues | 14 |
| Details | binding site for Ligand DAH C 123 bound to SER C 122 |
| Chain | Residue |
| C | LEU81 |
| C | THR82 |
| C | ASP85 |
| C | HIS119 |
| C | ALA120 |
| C | ARG121 |
| C | SER122 |
| C | GLY124 |
| C | THR125 |
| C | ILE126 |
| C | PHE127 |
| C | PHE184 |
| C | ILE206 |
| C | HOH501 |
| site_id | AD9 |
| Number of Residues | 15 |
| Details | binding site for Ligand residues DAH D 123 through GLY D 124 bound to SER D 122 |
| Chain | Residue |
| C | ASN30 |
| D | LEU81 |
| D | THR82 |
| D | ASP85 |
| D | HIS119 |
| D | ALA120 |
| D | ARG121 |
| D | SER122 |
| D | THR125 |
| D | ILE126 |
| D | PHE127 |
| D | SER128 |
| D | PHE184 |
| D | HOH501 |
| D | HOH505 |
