1YRH
Crystal Structure Of Trp Repressor Binding Protein Wrba in complex with FMN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| A | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016020 | cellular_component | membrane |
| C | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016020 | cellular_component | membrane |
| D | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| E | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| E | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016020 | cellular_component | membrane |
| E | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| F | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| F | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016020 | cellular_component | membrane |
| F | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| G | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| G | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016020 | cellular_component | membrane |
| G | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| H | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| H | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016020 | cellular_component | membrane |
| H | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN D 401 |
| Chain | Residue |
| A | HIS142 |
| D | THR86 |
| D | ARG87 |
| D | PHE88 |
| D | SER121 |
| D | ALA122 |
| D | GLN123 |
| D | ASN124 |
| D | GLY127 |
| D | HOH410 |
| B | TYR152 |
| D | SER13 |
| D | SER14 |
| D | THR15 |
| D | GLY16 |
| D | THR17 |
| D | GLY18 |
| D | PRO85 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN C 402 |
| Chain | Residue |
| A | TYR152 |
| B | HIS142 |
| C | SER13 |
| C | SER14 |
| C | THR15 |
| C | GLY16 |
| C | THR17 |
| C | GLY18 |
| C | PRO85 |
| C | THR86 |
| C | ARG87 |
| C | PHE88 |
| C | SER121 |
| C | ALA122 |
| C | GLN123 |
| C | ASN124 |
| C | GLY127 |
| C | ALA171 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN B 403 |
| Chain | Residue |
| B | SER13 |
| B | SER14 |
| B | THR15 |
| B | GLY16 |
| B | THR17 |
| B | GLY18 |
| B | PRO85 |
| B | THR86 |
| B | ARG87 |
| B | PHE88 |
| B | GLY89 |
| B | SER121 |
| B | ALA122 |
| B | GLN123 |
| B | ASN124 |
| B | GLY127 |
| C | ASP100 |
| C | HIS142 |
| D | TYR152 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN A 404 |
| Chain | Residue |
| A | SER13 |
| A | SER14 |
| A | THR15 |
| A | GLY16 |
| A | THR17 |
| A | GLY18 |
| A | PRO85 |
| A | THR86 |
| A | ARG87 |
| A | PHE88 |
| A | GLY89 |
| A | SER121 |
| A | ALA122 |
| A | GLN123 |
| A | ASN124 |
| A | GLY127 |
| D | HIS142 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN H 405 |
| Chain | Residue |
| E | HIS142 |
| H | SER13 |
| H | SER14 |
| H | THR15 |
| H | GLY16 |
| H | THR17 |
| H | GLY18 |
| H | PRO85 |
| H | THR86 |
| H | ARG87 |
| H | PHE88 |
| H | GLY89 |
| H | SER121 |
| H | ALA122 |
| H | GLN123 |
| H | ASN124 |
| H | GLY127 |
| H | ALA171 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN G 406 |
| Chain | Residue |
| G | THR86 |
| G | ARG87 |
| G | PHE88 |
| G | SER121 |
| G | ALA122 |
| G | GLN123 |
| G | ASN124 |
| G | GLY127 |
| G | HOH417 |
| E | TYR152 |
| F | HIS142 |
| G | SER13 |
| G | SER14 |
| G | THR15 |
| G | GLY16 |
| G | THR17 |
| G | GLY18 |
| G | PRO85 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN F 407 |
| Chain | Residue |
| F | SER13 |
| F | SER14 |
| F | THR15 |
| F | GLY16 |
| F | THR17 |
| F | GLY18 |
| F | PRO85 |
| F | THR86 |
| F | ARG87 |
| F | PHE88 |
| F | GLY89 |
| F | SER121 |
| F | ALA122 |
| F | GLN123 |
| F | ASN124 |
| F | GLY127 |
| F | HOH425 |
| G | ASP100 |
| G | HIS142 |
| H | TYR152 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN E 408 |
| Chain | Residue |
| E | SER13 |
| E | SER14 |
| E | THR15 |
| E | GLY16 |
| E | THR17 |
| E | GLY18 |
| E | PRO85 |
| E | THR86 |
| E | ARG87 |
| E | PHE88 |
| E | SER121 |
| E | ALA122 |
| E | GLN123 |
| E | ASN124 |
| E | GLY127 |
| G | TYR152 |
| H | ASP100 |
| H | HIS142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 112 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16322580","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






