Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005829 | cellular_component | cytosol |
A | 0006771 | biological_process | riboflavin metabolic process |
A | 0008270 | molecular_function | zinc ion binding |
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 | 0016310 | biological_process | phosphorylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0005829 | cellular_component | cytosol |
B | 0006771 | biological_process | riboflavin metabolic process |
B | 0008270 | molecular_function | zinc ion binding |
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 | 0016310 | biological_process | phosphorylation |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | SER38 |
A | THR45 |
A | ADP301 |
A | HOH569 |
A | HOH640 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | SER38 |
B | THR45 |
B | ASN47 |
B | ADP401 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | VAL30 |
A | HIS32 |
A | GLY33 |
A | GLY35 |
A | GLY37 |
A | SER38 |
A | LYS39 |
A | PRO44 |
A | THR45 |
A | ALA46 |
A | VAL97 |
A | LEU99 |
A | ARG102 |
A | ASP106 |
A | PHE107 |
A | TYR108 |
A | ZN501 |
A | HOH504 |
A | HOH529 |
A | HOH553 |
A | HOH622 |
B | TYR88 |
site_id | AC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE ADP B 401 |
Chain | Residue |
A | TYR88 |
B | GLY35 |
B | ARG36 |
B | GLY37 |
B | SER38 |
B | LYS39 |
B | PRO44 |
B | THR45 |
B | ALA46 |
B | VAL97 |
B | HIS98 |
B | LEU99 |
B | ARG102 |
B | ASP106 |
B | PHE107 |
B | TYR108 |
B | ZN601 |
B | HOH609 |
B | HOH615 |
B | HOH616 |
B | HOH643 |
B | HOH645 |
B | HOH652 |
B | HOH657 |
B | HOH666 |
B | HOH688 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000305 |
Chain | Residue | Details |
A | GLU96 | |
B | GLU96 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | THR45 | |
B | THR45 | |