1DFG
X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND BENZO-DIAZABORINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070404 | molecular_function | NADH binding |
| A | 1902494 | cellular_component | catalytic complex |
| B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0070404 | molecular_function | NADH binding |
| B | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | NDT0 |
| A | SER91 |
| A | ILE92 |
| A | SER145 |
| A | LYS163 |
| A | ALA189 |
| A | GLY190 |
| A | PRO191 |
| A | ILE192 |
| A | GLY13 |
| A | ALA15 |
| A | SER19 |
| A | ILE20 |
| A | GLN40 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NDT A 0 |
| Chain | Residue |
| A | GLY93 |
| A | PHE94 |
| A | ALA95 |
| A | LEU100 |
| A | TYR146 |
| A | TYR156 |
| A | MET159 |
| A | LYS163 |
| A | ILE200 |
| A | NAD501 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | NDT0 |
| B | GLY13 |
| B | VAL14 |
| B | ALA15 |
| B | SER19 |
| B | ILE20 |
| B | GLN40 |
| B | CYS63 |
| B | ASP64 |
| B | VAL65 |
| B | SER91 |
| B | ILE92 |
| B | GLY93 |
| B | LEU144 |
| B | SER145 |
| B | LYS163 |
| B | ALA189 |
| B | GLY190 |
| B | PRO191 |
| B | ILE192 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NDT B 0 |
| Chain | Residue |
| B | GLY93 |
| B | PHE94 |
| B | ALA95 |
| B | LEU100 |
| B | TYR156 |
| B | MET159 |
| B | LYS163 |
| B | NAD501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10201369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10398587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10595560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11514139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12109908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12699381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8953047","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Site: {"description":"Involved in acyl-ACP binding"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | GLU150 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | GLU150 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | TYR156 | |
| A | LYS163 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | TYR156 | |
| B | LYS163 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | MET159 | |
| A | LYS163 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | MET159 | |
| B | LYS163 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| A | TYR156 | proton acceptor, proton donor |
| A | LYS163 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| B | TYR156 | proton acceptor, proton donor |
| B | LYS163 | electrostatic stabiliser |
