1ICR
THE STRUCTURE OF ESCHERICHIA COLI NITROREDUCTASE COMPLEXED WITH NICOTINIC ACID
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 601 |
| Chain | Residue |
| A | ARG10 |
| A | GLU165 |
| A | GLY166 |
| A | ASN200 |
| A | LYS205 |
| A | ARG207 |
| A | HOH621 |
| A | HOH623 |
| A | HOH645 |
| A | HOH655 |
| B | PRO38 |
| A | HIS11 |
| B | SER39 |
| B | SER40 |
| B | ASN42 |
| B | GLN142 |
| B | LEU145 |
| B | NIO602 |
| A | SER12 |
| A | LYS14 |
| A | ASN71 |
| A | LYS74 |
| A | TYR144 |
| A | PRO163 |
| A | ILE164 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NIO B 602 |
| Chain | Residue |
| A | FMN601 |
| B | SER40 |
| B | THR41 |
| B | PHE124 |
| B | HOH854 |
| B | HOH858 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 603 |
| Chain | Residue |
| A | PRO38 |
| A | SER39 |
| A | SER40 |
| A | ASN42 |
| A | LEU145 |
| A | NIO604 |
| B | ARG10 |
| B | HIS11 |
| B | SER12 |
| B | LYS14 |
| B | LYS74 |
| B | TYR144 |
| B | PRO163 |
| B | ILE164 |
| B | GLU165 |
| B | GLY166 |
| B | ASN200 |
| B | LYS205 |
| B | ARG207 |
| B | HOH630 |
| B | HOH632 |
| B | HOH635 |
| B | HOH665 |
| B | HOH765 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NIO A 604 |
| Chain | Residue |
| A | SER40 |
| A | THR41 |
| A | PHE124 |
| A | HOH836 |
| B | FMN603 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11020276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q01234","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
