5I1V
Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 600 |
| Chain | Residue |
| A | ASP23 |
| A | ALA100 |
| A | GLY122 |
| A | PHE123 |
| A | VAL127 |
| A | GLY128 |
| A | GLY130 |
| A | GLY131 |
| A | HIS132 |
| A | GLY137 |
| A | TYR138 |
| A | VAL59 |
| A | GLY191 |
| A | GLY192 |
| A | GLY195 |
| A | ILE197 |
| A | TYR446 |
| A | ASN448 |
| A | TYR449 |
| A | HOH788 |
| A | HOH842 |
| A | HOH868 |
| A | ARG60 |
| A | HOH919 |
| A | HOH920 |
| A | SER61 |
| A | GLY62 |
| A | GLY63 |
| A | HIS64 |
| A | VAL70 |
| A | LEU81 |
| site_id | AC2 |
| Number of Residues | 32 |
| Details | binding site for residue FAD B 600 |
| Chain | Residue |
| B | ASP23 |
| B | VAL59 |
| B | ARG60 |
| B | SER61 |
| B | GLY62 |
| B | GLY63 |
| B | HIS64 |
| B | PHE69 |
| B | VAL70 |
| B | LEU81 |
| B | ALA100 |
| B | GLY122 |
| B | PHE123 |
| B | VAL127 |
| B | GLY128 |
| B | GLY131 |
| B | HIS132 |
| B | GLY137 |
| B | TYR138 |
| B | GLY191 |
| B | GLY192 |
| B | GLY195 |
| B | ILE197 |
| B | TYR446 |
| B | ASN448 |
| B | TYR449 |
| B | HOH856 |
| B | HOH866 |
| B | HOH905 |
| B | HOH910 |
| B | HOH911 |
| B | HOH958 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 600 |
| Chain | Residue |
| C | ASP23 |
| C | VAL59 |
| C | ARG60 |
| C | SER61 |
| C | GLY62 |
| C | GLY63 |
| C | HIS64 |
| C | PHE69 |
| C | VAL70 |
| C | LEU81 |
| C | ALA100 |
| C | GLY122 |
| C | PHE123 |
| C | VAL127 |
| C | GLY128 |
| C | GLY131 |
| C | HIS132 |
| C | GLY137 |
| C | TYR138 |
| C | GLY191 |
| C | GLY192 |
| C | GLY195 |
| C | ILE197 |
| C | TYR446 |
| C | ASN448 |
| C | TYR449 |
| C | HOH893 |
| C | HOH915 |
| C | HOH928 |
| C | HOH960 |
| C | HOH1014 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD D 600 |
| Chain | Residue |
| D | GLY63 |
| D | HIS64 |
| D | PHE69 |
| D | VAL70 |
| D | LEU81 |
| D | ALA100 |
| D | GLY122 |
| D | PHE123 |
| D | VAL127 |
| D | GLY128 |
| D | GLY131 |
| D | HIS132 |
| D | GLY137 |
| D | TYR138 |
| D | GLY191 |
| D | GLY192 |
| D | GLY195 |
| D | ILE197 |
| D | TYR446 |
| D | ASN448 |
| D | TYR449 |
| D | HOH891 |
| D | HOH892 |
| D | HOH904 |
| D | HOH917 |
| D | HOH956 |
| D | ASP23 |
| D | VAL59 |
| D | ARG60 |
| D | SER61 |
| D | GLY62 |
