5F12
WrbA in complex with FMN under crystallization conditions of WrbA-FMN-BQ structure (4YQE)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050136 | molecular_function | NADH dehydrogenase (quinone) (non-electrogenic) activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue FMN A 201 |
| Chain | Residue |
| A | SER9 |
| A | PHE79 |
| A | SER112 |
| A | THR113 |
| A | GLY114 |
| A | THR115 |
| A | GLY116 |
| A | GLY117 |
| A | HOH305 |
| A | HOH337 |
| B | ASP91 |
| A | MHO10 |
| B | HIS132 |
| A | TYR11 |
| A | GLY12 |
| A | HIS13 |
| A | ILE14 |
| A | PRO76 |
| A | THR77 |
| A | ARG78 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue FMN B 201 |
| Chain | Residue |
| A | ASP91 |
| A | HIS132 |
| B | SER9 |
| B | MHO10 |
| B | TYR11 |
| B | GLY12 |
| B | HIS13 |
| B | ILE14 |
| B | PRO76 |
| B | THR77 |
| B | ARG78 |
| B | PHE79 |
| B | SER112 |
| B | THR113 |
| B | GLY114 |
| B | THR115 |
| B | GLY116 |
| B | GLY117 |
| B | ALA165 |
| B | HOH306 |
| B | HOH326 |
| B | HOH333 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17951395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01017","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17951395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19665595","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01017","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17951395","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
