3B6M
WrbA from Escherichia coli, second crystal form
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 | 20 |
Details | BINDING SITE FOR RESIDUE FMN A 200 |
Chain | Residue |
A | SER10 |
A | PHE80 |
A | ASP92 |
A | SER113 |
A | THR114 |
A | GLY115 |
A | THR116 |
A | GLY117 |
A | GLY118 |
A | HIS133 |
A | 144201 |
A | MET11 |
A | HOH216 |
A | TYR12 |
A | GLY13 |
A | HIS14 |
A | ILE15 |
A | PRO77 |
A | THR78 |
A | ARG79 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE FMN B 200 |
Chain | Residue |
B | SER10 |
B | MET11 |
B | TYR12 |
B | GLY13 |
B | HIS14 |
B | ILE15 |
B | PRO77 |
B | THR78 |
B | ARG79 |
B | PHE80 |
B | ASP92 |
B | SER113 |
B | THR114 |
B | GLY115 |
B | THR116 |
B | GLY117 |
B | GLY118 |
B | HIS133 |
B | 144201 |
B | HOH250 |
B | HOH311 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 144 A 201 |
Chain | Residue |
A | TRP98 |
A | THR116 |
A | GLY118 |
A | HIS133 |
A | FMN200 |
B | TYR143 |
B | PRO159 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 144 B 201 |
Chain | Residue |
A | TYR143 |
A | GLN146 |
A | PRO159 |
B | TRP98 |
B | THR116 |
B | GLY118 |
B | HIS133 |
B | FMN200 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 15P A 202 |
Chain | Residue |
A | TYR188 |
A | GLY191 |
A | LEU192 |
A | LYS195 |
A | HOH213 |
B | GLY105 |
B | LEU196 |
B | ASN197 |
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 | SER10 | |
A | THR78 | |
A | SER113 | |
A | HIS133 | |
B | SER10 | |
B | THR78 | |
B | SER113 | |
B | HIS133 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17951395 |
Chain | Residue | Details |
A | TYR12 | |
A | ALA51 | |
A | ASP169 | |
B | TYR12 | |
B | ALA51 | |
B | ASP169 |
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 | TRP98 | |
B | TRP98 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS50 | |
B | LYS50 |