3B6K
WrbA from Escherichia coli, Benzoquinone complex
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 | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 200 |
| Chain | Residue |
| A | SER10 |
| A | PHE80 |
| A | SER113 |
| A | THR114 |
| A | GLY115 |
| A | THR116 |
| A | GLY117 |
| A | GLY118 |
| A | PLQ201 |
| A | HOH251 |
| A | HOH252 |
| A | MET11 |
| A | HOH253 |
| A | HOH379 |
| B | ASP92 |
| B | HIS133 |
| A | TYR12 |
| A | GLY13 |
| A | HIS14 |
| A | ILE15 |
| A | PRO77 |
| A | THR78 |
| A | ARG79 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 200 |
| Chain | Residue |
| A | ASP92 |
| A | HIS133 |
| B | SER10 |
| B | MET11 |
| B | TYR12 |
| B | GLY13 |
| B | HIS14 |
| B | ILE15 |
| B | PRO77 |
| B | THR78 |
| B | ARG79 |
| B | PHE80 |
| B | SER113 |
| B | THR114 |
| B | GLY115 |
| B | THR116 |
| B | GLY117 |
| B | GLY118 |
| B | PLQ201 |
| B | HOH271 |
| B | HOH272 |
| B | HOH273 |
| B | HOH399 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PLQ A 201 |
| Chain | Residue |
| A | FMN200 |
| A | HOH384 |
| A | HOH385 |
| A | HOH388 |
| A | HOH389 |
| B | GLY95 |
| B | TRP98 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PLQ B 201 |
| Chain | Residue |
| A | TRP98 |
| B | FMN200 |
| B | HOH403 |
| B | HOH408 |
| B | HOH410 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 15P B 202 |
| Chain | Residue |
| A | TYR143 |
| A | ALA144 |
| A | PHE149 |
| B | TRP98 |
| B | ALA99 |
| B | SER100 |
| B | GLY101 |
| B | HOH263 |
| B | HOH359 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 15P A 202 |
| Chain | Residue |
| A | TRP98 |
| A | ALA99 |
| A | SER100 |
| A | GLY101 |
| A | HOH370 |
| B | TYR143 |
| B | ALA144 |
| B | GLN146 |
| B | HOH364 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 15P B 203 |
| Chain | Residue |
| A | GLU49 |
| A | LYS50 |
| A | GLY52 |
| A | GLY53 |
| A | GLY105 |
| A | LEU196 |
| A | ASN197 |
| A | HOH327 |
| B | TYR188 |
| B | LEU192 |
| B | LYS195 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 15P A 203 |
| Chain | Residue |
| A | TYR188 |
| A | LEU192 |
| A | LYS195 |
| A | HOH322 |
| A | HOH395 |
| B | ASN197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 370 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_01017","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| 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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17951395","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
