3X22
Crystal structure of Escherichia coli nitroreductase NfsB mutant N71S/F123A/F124W
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
A | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
A | 0005829 | cellular_component | cytosol |
A | 0010181 | molecular_function | FMN binding |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
A | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
B | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
B | 0005829 | cellular_component | cytosol |
B | 0010181 | molecular_function | FMN binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046256 | biological_process | 2,4,6-trinitrotoluene catabolic process |
B | 0046857 | molecular_function | oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FMN A 301 |
Chain | Residue |
A | ARG10 |
A | GLY166 |
A | ASN200 |
A | LYS205 |
A | ARG207 |
A | HOH413 |
A | HOH423 |
A | HOH424 |
A | HOH453 |
A | HOH492 |
B | PRO38 |
A | HIS11 |
B | SER39 |
B | SER40 |
B | ASN42 |
B | TRP124 |
B | GLN142 |
B | LEU145 |
B | HOH435 |
A | SER12 |
A | LYS14 |
A | LYS74 |
A | TYR144 |
A | PRO163 |
A | ILE164 |
A | GLU165 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FMN B 301 |
Chain | Residue |
A | PRO38 |
A | SER39 |
A | SER40 |
A | ASN42 |
A | TRP124 |
A | GLN142 |
A | LEU145 |
B | ARG10 |
B | HIS11 |
B | SER12 |
B | LYS14 |
B | LYS74 |
B | PRO163 |
B | ILE164 |
B | GLU165 |
B | GLY166 |
B | ASN200 |
B | LYS205 |
B | ARG207 |
B | HOH409 |
B | HOH423 |
B | HOH427 |
B | HOH452 |
B | HOH480 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11020276, ECO:0000269|PubMed:11491290, ECO:0000269|PubMed:15684426 |
Chain | Residue | Details |
A | ARG10 | |
A | GLU165 | |
A | LYS205 | |
B | ARG10 | |
B | GLU165 | |
B | LYS205 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q01234 |
Chain | Residue | Details |
A | LYS14 | |
B | ARG107 | |
A | THR41 | |
A | SER71 | |
A | LYS74 | |
A | ARG107 | |
B | LYS14 | |
B | THR41 | |
B | SER71 | |
B | LYS74 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 211 |
Chain | Residue | Details |
A | LYS14 | electrostatic stabiliser, hydrogen bond donor |
A | LYS74 | electrostatic stabiliser, hydrogen bond donor |
A | GLU165 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 211 |
Chain | Residue | Details |
B | LYS14 | electrostatic stabiliser, hydrogen bond donor |
B | LYS74 | electrostatic stabiliser, hydrogen bond donor |
B | GLU165 | electrostatic stabiliser, hydrogen bond donor |