5MP4
The structure of Pst2p from Saccharomyces cerevisiae
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| E | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| F | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| G | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| H | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 201 |
| Chain | Residue |
| A | THR10 |
| A | LEU11 |
| A | TYR12 |
| A | GLY13 |
| A | HIS14 |
| A | VAL15 |
| A | PRO77 |
| A | SER113 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 201 |
| Chain | Residue |
| B | LEU11 |
| B | TYR12 |
| B | GLY13 |
| B | HIS14 |
| B | VAL15 |
| B | PRO77 |
| B | SER113 |
| B | THR10 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 C 201 |
| Chain | Residue |
| C | THR10 |
| C | LEU11 |
| C | TYR12 |
| C | GLY13 |
| C | HIS14 |
| C | VAL15 |
| C | PRO77 |
| C | SER113 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 D 201 |
| Chain | Residue |
| D | THR10 |
| D | LEU11 |
| D | TYR12 |
| D | GLY13 |
| D | HIS14 |
| D | VAL15 |
| D | PRO77 |
| D | SER113 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 E 201 |
| Chain | Residue |
| E | THR10 |
| E | LEU11 |
| E | TYR12 |
| E | GLY13 |
| E | HIS14 |
| E | VAL15 |
| E | PRO77 |
| E | SER113 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 F 201 |
| Chain | Residue |
| F | THR10 |
| F | LEU11 |
| F | TYR12 |
| F | GLY13 |
| F | HIS14 |
| F | VAL15 |
| F | PRO77 |
| F | SER113 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 G 201 |
| Chain | Residue |
| G | THR10 |
| G | LEU11 |
| G | TYR12 |
| G | GLY13 |
| G | HIS14 |
| G | VAL15 |
| G | PRO77 |
| G | SER113 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 H 201 |
| Chain | Residue |
| H | THR10 |
| H | LEU11 |
| H | TYR12 |
| H | GLY13 |
| H | HIS14 |
| H | VAL15 |
| H | PRO77 |
| H | SER113 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1352 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
