2ED4
Crystal structure of flavin reductase HpaC complexed with FAD and NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| A | 0009056 | biological_process | catabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016646 | molecular_function | oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor |
| A | 0036382 | molecular_function | flavin reductase (NADH) activity |
| A | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
| B | 0006208 | biological_process | pyrimidine nucleobase catabolic process |
| B | 0009056 | biological_process | catabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016646 | molecular_function | oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor |
| B | 0036382 | molecular_function | flavin reductase (NADH) activity |
| B | 0042602 | molecular_function | riboflavin reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 400 |
| Chain | Residue |
| A | GLU27 |
| A | VAL49 |
| A | SER50 |
| A | ALA53 |
| A | LYS54 |
| A | LEU55 |
| A | HIS80 |
| A | PHE81 |
| A | ALA82 |
| A | GLY83 |
| A | ARG84 |
| A | ARG28 |
| A | PRO85 |
| A | HIS116 |
| A | NAD401 |
| A | HOH435 |
| A | HOH440 |
| A | HOH445 |
| A | HOH497 |
| A | GLY29 |
| A | MET30 |
| A | THR31 |
| A | ALA32 |
| A | THR33 |
| A | ALA34 |
| A | ALA48 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | LYS6 |
| A | LEU9 |
| A | THR33 |
| A | HIS116 |
| A | TYR137 |
| A | ARG140 |
| A | FAD400 |
| A | HOH411 |
| A | HOH415 |
| A | HOH425 |
| A | HOH449 |
| A | HOH453 |
| A | HOH505 |
| A | HOH510 |
| B | SER37 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 500 |
| Chain | Residue |
| B | GLU27 |
| B | ARG28 |
| B | GLY29 |
| B | MET30 |
| B | THR31 |
| B | ALA32 |
| B | THR33 |
| B | ALA34 |
| B | ALA48 |
| B | VAL49 |
| B | SER50 |
| B | ALA53 |
| B | LYS54 |
| B | LEU55 |
| B | HIS80 |
| B | PHE81 |
| B | ALA82 |
| B | GLY83 |
| B | ARG84 |
| B | PRO85 |
| B | LEU91 |
| B | HIS116 |
| B | TYR137 |
| B | NAD501 |
| B | HOH513 |
| B | HOH515 |
| B | HOH519 |
| B | HOH532 |
| B | HOH548 |
| B | HOH573 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| A | SER37 |
| A | HOH408 |
| B | LYS6 |
| B | LEU9 |
| B | THR33 |
| B | HIS116 |
| B | TYR137 |
| B | ARG140 |
| B | FAD500 |
| B | HOH504 |
| B | HOH509 |
| B | HOH511 |
| B | HOH516 |
| B | HOH528 |
| B | HOH530 |
| B | HOH551 |
| B | HOH556 |
| B | HOH611 |
| B | HOH629 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17729270, ECO:0007744|PDB:2ED4 |
| Chain | Residue | Details |
| A | GLU27 | |
| B | ALA48 | |
| B | LYS54 | |
| B | HIS80 | |
| B | HIS116 | |
| B | TYR137 | |
| A | SER37 | |
| A | ALA48 | |
| A | LYS54 | |
| A | HIS80 | |
| A | HIS116 | |
| A | TYR137 | |
| B | GLU27 | |
| B | SER37 |
