3ZHO
X-ray structure of E.coli Wrba in complex with FMN at 1.2 A resolution
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 1198 |
Chain | Residue |
A | SER9 |
A | PHE79 |
A | GLY80 |
A | SER112 |
A | THR113 |
A | GLY114 |
A | THR115 |
A | GLY116 |
A | GLY117 |
A | HOH2088 |
A | HOH2145 |
A | SME10 |
A | HOH2170 |
B | ASP91 |
B | HIS132 |
A | TYR11 |
A | GLY12 |
A | HIS13 |
A | ILE14 |
A | PRO76 |
A | THR77 |
A | ARG78 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FMN B 1198 |
Chain | Residue |
A | ASP91 |
A | HIS132 |
B | SER9 |
B | SME10 |
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 | HOH2094 |
B | HOH2116 |
B | HOH2146 |
B | HOH2147 |
B | HOH2148 |
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 |