5TRD
Structure of RbkR (Riboflavin Kinase) from Thermoplasma acidophilum determined in complex with CTP and its cognate DNA operator
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008531 | molecular_function | riboflavin kinase activity |
| A | 0009231 | biological_process | riboflavin biosynthetic process |
| A | 0009398 | biological_process | FMN biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008531 | molecular_function | riboflavin kinase activity |
| B | 0009231 | biological_process | riboflavin biosynthetic process |
| B | 0009398 | biological_process | FMN biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue CTP A 301 |
| Chain | Residue |
| A | SER101 |
| A | THR131 |
| A | LEU132 |
| A | ASN133 |
| A | LYS200 |
| A | TYR201 |
| A | LEU202 |
| A | ARG203 |
| A | NA302 |
| A | HOH408 |
| A | HOH431 |
| A | GLY102 |
| A | HOH444 |
| A | HOH450 |
| A | HOH451 |
| A | HOH482 |
| A | HOH496 |
| A | HOH498 |
| A | MET103 |
| A | GLY104 |
| A | GLU105 |
| A | GLY106 |
| A | ARG107 |
| A | TYR128 |
| A | GLY130 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | THR131 |
| A | ASN133 |
| A | CTP301 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue CTP B 301 |
| Chain | Residue |
| B | SER101 |
| B | GLY102 |
| B | MET103 |
| B | GLY104 |
| B | GLU105 |
| B | GLY106 |
| B | ARG107 |
| B | TYR128 |
| B | GLY130 |
| B | THR131 |
| B | LEU132 |
| B | ASN133 |
| B | SER198 |
| B | LYS200 |
| B | TYR201 |
| B | LEU202 |
| B | ARG203 |
| B | NA302 |
| B | HOH401 |
| B | HOH405 |
| B | HOH407 |
| B | HOH414 |
| B | HOH441 |
| B | HOH449 |
| B | HOH450 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| B | THR131 |
| B | ASN133 |
| B | CTP301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 254 |
| Details | Region: {"description":"Riboflavin kinase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
