4YQE
Crystal structure of E. coli WrbA in complex with benzoquinone
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:ubiquinone reductase (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:ubiquinone reductase (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 | 22 |
| Details | binding site for residue FMN A 201 |
| Chain | Residue |
| A | SER9 |
| A | PHE79 |
| A | GLY80 |
| A | SER112 |
| A | THR113 |
| A | GLY114 |
| A | THR115 |
| A | GLY116 |
| A | GLY117 |
| A | HOH328 |
| A | HOH329 |
| A | MHO10 |
| B | ASP91 |
| B | HIS132 |
| B | PLQ201 |
| A | TYR11 |
| A | GLY12 |
| A | HIS13 |
| A | ILE14 |
| A | PRO76 |
| A | THR77 |
| A | ARG78 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PLQ A 202 |
| Chain | Residue |
| A | TRP97 |
| A | HIS132 |
| A | TYR142 |
| B | PHE79 |
| B | FMN202 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue PLQ B 201 |
| Chain | Residue |
| A | PHE79 |
| A | FMN201 |
| B | TRP97 |
| B | HIS132 |
| B | TYR142 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue FMN B 202 |
| Chain | Residue |
| A | ASP91 |
| A | HIS132 |
| A | PLQ202 |
| B | SER9 |
| B | MHO10 |
| B | TYR11 |
| B | GLY12 |
| B | HIS13 |
| B | ILE14 |
| B | PRO76 |
| B | THR77 |
| B | ARG78 |
| B | PHE79 |
| B | GLY80 |
| B | SER112 |
| B | THR113 |
| B | GLY114 |
| B | THR115 |
| B | GLY116 |
| B | GLY117 |
| B | HOH304 |
| B | HOH312 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for Ligand residues MHO A 10 through TYR A 11 bound to SER A 9 |
| Chain | Residue |
| A | TYR8 |
| A | SER9 |
| A | GLY12 |
| A | HIS13 |
| A | PHE47 |
| A | ALA50 |
| A | GLY51 |
| A | GLY52 |
| A | LYS53 |
| A | ARG78 |
| A | FMN201 |
| A | HOH331 |
| A | HOH340 |
| A | HOH341 |
| A | HOH370 |
| A | HOH388 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for Ligand residues MHO B 10 through TYR B 11 bound to SER B 9 |
| Chain | Residue |
| B | TYR8 |
| B | SER9 |
| B | GLY12 |
| B | HIS13 |
| B | MET42 |
| B | PHE47 |
| B | ALA50 |
| B | GLY51 |
| B | GLY52 |
| B | LYS53 |
| B | ARG78 |
| B | FMN202 |
| B | HOH336 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595 |
| Chain | Residue | Details |
| A | SER9 | |
| A | THR77 | |
| A | SER112 | |
| A | HIS132 | |
| B | SER9 | |
| B | THR77 | |
| B | SER112 | |
| B | HIS132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17951395 |
| Chain | Residue | Details |
| A | TYR11 | |
| A | ALA50 | |
| A | ASP168 | |
| B | TYR11 | |
| B | ALA50 | |
| B | ASP168 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000305|PubMed:17951395 |
| Chain | Residue | Details |
| A | TRP97 | |
| B | TRP97 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS49 | |
| B | LYS49 |
