3B6J
WrbA from Escherichia coli, NADH 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 | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 200 |
| Chain | Residue |
| A | SER10 |
| A | PHE80 |
| A | GLY81 |
| A | SER113 |
| A | THR114 |
| A | GLY115 |
| A | THR116 |
| A | GLY117 |
| A | GLY118 |
| A | NAD201 |
| A | 15P202 |
| A | MET11 |
| A | HOH256 |
| A | HOH257 |
| A | HOH369 |
| 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 | THR78 |
| B | ARG79 |
| B | PHE80 |
| B | SER113 |
| B | THR114 |
| B | GLY115 |
| B | THR116 |
| B | GLY117 |
| B | GLY118 |
| B | NAD201 |
| B | 15P203 |
| B | HOH218 |
| B | HOH269 |
| B | HOH270 |
| B | HOH272 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 201 |
| Chain | Residue |
| A | TYR12 |
| A | MET43 |
| A | ALA51 |
| A | GLN86 |
| A | ASP169 |
| A | GLY170 |
| A | FMN200 |
| A | 15P202 |
| A | HOH205 |
| A | HOH258 |
| A | HOH259 |
| A | HOH260 |
| A | HOH261 |
| A | HOH319 |
| A | HOH320 |
| A | HOH350 |
| A | HOH351 |
| A | HOH358 |
| B | ASP92 |
| B | GLN93 |
| B | GLY95 |
| B | 15P205 |
| B | HOH220 |
| B | HOH229 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD B 201 |
| Chain | Residue |
| A | ASP92 |
| A | GLN93 |
| A | GLY95 |
| A | HOH214 |
| B | TYR12 |
| B | MET43 |
| B | ALA51 |
| B | ASP169 |
| B | GLY170 |
| B | FMN200 |
| B | 15P203 |
| B | HOH231 |
| B | HOH252 |
| B | HOH257 |
| B | HOH271 |
| B | HOH272 |
| B | HOH308 |
| B | HOH309 |
| B | HOH310 |
| B | HOH350 |
| B | HOH381 |
| B | HOH385 |
| B | HOH386 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AMP B 202 |
| Chain | Residue |
| B | GLN146 |
| B | GLU147 |
| B | SER180 |
| B | TYR184 |
| B | GLU187 |
| A | LYS54 |
| A | THR57 |
| A | HOH242 |
| B | ALA144 |
| B | ALA145 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 15P A 202 |
| Chain | Residue |
| A | PHE80 |
| A | TYR143 |
| A | FMN200 |
| A | NAD201 |
| A | HOH350 |
| A | HOH351 |
| A | HOH357 |
| B | GLY95 |
| B | TRP98 |
| B | HIS133 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 15P B 203 |
| Chain | Residue |
| A | GLY95 |
| A | TRP98 |
| A | HIS133 |
| B | PHE80 |
| B | TYR143 |
| B | FMN200 |
| B | NAD201 |
| B | HOH381 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 15P B 204 |
| Chain | Residue |
| A | ALA144 |
| A | GLN146 |
| B | TRP98 |
| B | ALA99 |
| B | SER100 |
| B | GLY101 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 15P A 203 |
| Chain | Residue |
| A | TRP98 |
| A | ALA99 |
| A | SER100 |
| A | GLY101 |
| A | TYR104 |
| B | GLN146 |
| B | PHE149 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 15P B 205 |
| Chain | Residue |
| A | GLU49 |
| A | LYS50 |
| A | ALA51 |
| A | GLY52 |
| A | GLY53 |
| A | GLY105 |
| A | LEU196 |
| A | ASN197 |
| A | NAD201 |
| B | TYR188 |
| B | LEU192 |
| B | LYS195 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 15P A 204 |
| Chain | Residue |
| A | TYR188 |
| A | LEU192 |
| A | LYS195 |
| 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 |
