1Q9S
Crystal structure of riboflavin kinase with ternary product complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005829 | cellular_component | cytosol |
| A | 0006771 | biological_process | riboflavin metabolic process |
| A | 0006915 | biological_process | apoptotic process |
| 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 | 0033864 | biological_process | positive regulation of NAD(P)H oxidase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 201 |
| Chain | Residue |
| A | THR34 |
| A | ASN36 |
| A | ADP301 |
| A | FMN401 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 301 |
| Chain | Residue |
| A | SER27 |
| A | PRO33 |
| A | THR34 |
| A | ALA35 |
| A | ASN36 |
| A | THR87 |
| A | ILE89 |
| A | HIS91 |
| A | ASP96 |
| A | PHE97 |
| A | TYR98 |
| A | MG201 |
| A | FMN401 |
| A | HOH502 |
| A | HOH514 |
| A | HOH516 |
| A | HOH529 |
| A | VAL19 |
| A | GLY22 |
| A | PHE23 |
| A | GLY24 |
| A | GLY26 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | GLY22 |
| A | PHE23 |
| A | GLY24 |
| A | ARG25 |
| A | GLY26 |
| A | THR34 |
| A | ASN36 |
| A | ILE53 |
| A | VAL69 |
| A | SER71 |
| A | ASN75 |
| A | PRO76 |
| A | TYR77 |
| A | TYR78 |
| A | GLU86 |
| A | ARG111 |
| A | LYS114 |
| A | PHE116 |
| A | ILE126 |
| A | ASP129 |
| A | MG201 |
| A | ADP301 |
| A | HOH503 |
| A | HOH505 |
| A | HOH568 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12623014","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14580199","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NB0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NB9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P4M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q9S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14580199","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q9S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
