4JQC
Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AFN-1252
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 | 22 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | GLY13 |
| A | ILE92 |
| A | GLY93 |
| A | ILE119 |
| A | LEU144 |
| A | SER145 |
| A | LYS163 |
| A | ALA189 |
| A | GLY190 |
| A | ILE192 |
| A | THR194 |
| A | ALA15 |
| A | LEU195 |
| A | ALA196 |
| A | 0WE302 |
| A | ILE20 |
| A | GLN40 |
| A | LEU44 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
| A | SER91 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 0WE A 302 |
| Chain | Residue |
| A | PHE94 |
| A | ALA95 |
| A | GLY97 |
| A | TYR146 |
| A | ASN155 |
| A | TYR156 |
| A | ALA196 |
| A | SER198 |
| A | ILE200 |
| A | NAD301 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 301 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | SER19 |
| B | ILE20 |
| B | GLN40 |
| B | LEU44 |
| B | CYS63 |
| B | ASP64 |
| B | VAL65 |
| B | SER91 |
| B | ILE92 |
| B | GLY93 |
| B | ILE119 |
| B | SER145 |
| B | LYS163 |
| B | ALA189 |
| B | GLY190 |
| B | ILE192 |
| B | THR194 |
| B | LEU195 |
| B | ALA196 |
| B | 0WE302 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 0WE B 302 |
| Chain | Residue |
| B | PHE94 |
| B | ALA95 |
| B | GLY97 |
| B | ASN155 |
| B | TYR156 |
| B | SER198 |
| B | GLY199 |
| B | NAD301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR146 | |
| A | TYR156 | |
| B | TYR146 | |
| B | TYR156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047 |
| Chain | Residue | Details |
| A | GLY13 | |
| B | GLN40 | |
| B | ASP64 | |
| B | ILE92 | |
| B | LYS163 | |
| B | ILE192 | |
| A | SER19 | |
| A | GLN40 | |
| A | ASP64 | |
| A | ILE92 | |
| A | LYS163 | |
| A | ILE192 | |
| B | GLY13 | |
| B | SER19 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA95 | |
| B | ALA95 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | SITE: Involved in acyl-ACP binding |
| Chain | Residue | Details |
| A | LYS201 | |
| A | ARG204 | |
| A | LYS205 | |
| B | LYS201 | |
| B | ARG204 | |
| B | LYS205 |
