1DFI
X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD
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 | 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 | 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 |
| C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030497 | biological_process | fatty acid elongation |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0070404 | molecular_function | NADH binding |
| C | 1902494 | cellular_component | catalytic complex |
| D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0008610 | biological_process | lipid biosynthetic process |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030497 | biological_process | fatty acid elongation |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0070404 | molecular_function | NADH binding |
| D | 1902494 | cellular_component | catalytic complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | GLY13 |
| A | SER91 |
| A | ILE92 |
| A | LEU144 |
| A | SER145 |
| A | LYS163 |
| A | ALA189 |
| A | ILE192 |
| A | LEU195 |
| A | HOH539 |
| A | HOH541 |
| A | VAL14 |
| A | HOH591 |
| A | ALA15 |
| A | SER19 |
| A | ILE20 |
| A | GLN40 |
| A | CYS63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | GLY13 |
| B | ALA15 |
| B | SER19 |
| B | ILE20 |
| B | ALA21 |
| B | GLN40 |
| B | CYS63 |
| B | ASP64 |
| B | VAL65 |
| B | SER91 |
| B | ILE92 |
| B | LEU144 |
| B | SER145 |
| B | LYS163 |
| B | ALA189 |
| B | GLY190 |
| B | HOH528 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | GLY13 |
| C | ALA15 |
| C | ILE20 |
| C | GLN40 |
| C | CYS63 |
| C | ASP64 |
| C | VAL65 |
| C | SER91 |
| C | ILE92 |
| C | GLY93 |
| C | LEU144 |
| C | SER145 |
| C | LYS163 |
| C | ALA189 |
| C | GLY190 |
| C | ILE192 |
| C | LEU195 |
| C | HOH512 |
| C | HOH551 |
| C | HOH580 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAD D 501 |
| Chain | Residue |
| D | GLY13 |
| D | ALA15 |
| D | SER19 |
| D | ILE20 |
| D | GLN40 |
| D | CYS63 |
| D | ASP64 |
| D | VAL65 |
| D | SER91 |
| D | LEU144 |
| D | SER145 |
| D | LYS163 |
| D | ALA189 |
| D | GLY190 |
| D | PRO191 |
| D | ILE192 |
| D | LEU195 |
| D | HOH526 |
| D | HOH535 |
| D | HOH561 |
| D | HOH564 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU147 | |
| A | ASN157 | |
| B | LEU147 | |
| B | ASN157 | |
| C | LEU147 | |
| C | ASN157 | |
| D | LEU147 | |
| D | ASN157 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| 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 | VAL14 | |
| B | ASN41 | |
| B | VAL65 | |
| B | GLY93 | |
| B | ALA164 | |
| B | ARG193 | |
| C | VAL14 | |
| C | ILE20 | |
| C | ASN41 | |
| C | VAL65 | |
| C | GLY93 | |
| A | ILE20 | |
| C | ALA164 | |
| C | ARG193 | |
| D | VAL14 | |
| D | ILE20 | |
| D | ASN41 | |
| D | VAL65 | |
| D | GLY93 | |
| D | ALA164 | |
| D | ARG193 | |
| A | ASN41 | |
| A | VAL65 | |
| A | GLY93 | |
| A | ALA164 | |
| A | ARG193 | |
| B | VAL14 | |
| B | ILE20 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO96 | |
| B | PRO96 | |
| C | PRO96 | |
| D | PRO96 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | SITE: Involved in acyl-ACP binding |
| Chain | Residue | Details |
| A | ASP202 | |
| D | ASP202 | |
| D | LYS205 | |
| D | MET206 | |
| A | LYS205 | |
| A | MET206 | |
| B | ASP202 | |
| B | LYS205 | |
| B | MET206 | |
| C | ASP202 | |
| C | LYS205 | |
| C | MET206 |
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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | MET159 | |
| B | LYS163 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | MET159 | |
| C | LYS163 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | MET159 | |
| D | LYS163 |
| 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 | 1 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | GLU150 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | GLU150 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | TYR156 | |
| A | LYS163 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | TYR156 | |
| B | LYS163 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | TYR156 | |
| C | LYS163 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | TYR156 | |
| D | LYS163 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | MET159 | |
| A | LYS163 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| A | ASN157 | proton acceptor, proton donor |
| A | ALA164 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| B | ASN157 | proton acceptor, proton donor |
| B | ALA164 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| C | ASN157 | proton acceptor, proton donor |
| C | ALA164 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 606 |
| Chain | Residue | Details |
| D | ASN157 | proton acceptor, proton donor |
| D | ALA164 | electrostatic stabiliser |
