1QG6
CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN
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 | 0016631 | molecular_function | enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) |
| 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 | 0016631 | molecular_function | enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) |
| 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 | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0016631 | molecular_function | enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) |
| 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 | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0016631 | molecular_function | enoyl-[acyl-carrier-protein] reductase activity (NAD(P)H) |
| 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 | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | GLY13 |
| A | VAL65 |
| A | SER91 |
| A | ILE92 |
| A | GLY93 |
| A | LEU144 |
| A | SER145 |
| A | LYS163 |
| A | ALA189 |
| A | GLY190 |
| A | PRO191 |
| A | VAL14 |
| A | ILE192 |
| A | THR194 |
| A | ALA196 |
| A | TCL601 |
| A | HOH608 |
| A | HOH611 |
| A | HOH617 |
| A | HOH619 |
| A | HOH649 |
| A | HOH662 |
| A | ALA15 |
| A | HOH667 |
| A | SER19 |
| A | ILE20 |
| A | GLN40 |
| A | LEU44 |
| A | CYS63 |
| A | ASP64 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TCL A 601 |
| Chain | Residue |
| A | GLY93 |
| A | ALA95 |
| A | LEU100 |
| A | TYR146 |
| A | TYR156 |
| A | ALA196 |
| A | ILE200 |
| A | NAD501 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD B 502 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | ALA15 |
| B | SER19 |
| B | ILE20 |
| B | GLN40 |
| B | LEU44 |
| 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 |
| B | THR194 |
| B | ALA196 |
| B | TCL602 |
| B | HOH612 |
| B | HOH615 |
| B | HOH621 |
| B | HOH623 |
| B | HOH653 |
| B | HOH666 |
| B | HOH671 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TCL B 602 |
| Chain | Residue |
| B | GLY93 |
| B | ALA95 |
| B | LEU100 |
| B | TYR146 |
| B | TYR156 |
| B | ALA196 |
| B | ILE200 |
| B | NAD502 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD C 503 |
| Chain | Residue |
| C | HOH614 |
| C | HOH617 |
| C | HOH623 |
| C | HOH625 |
| C | HOH655 |
| C | HOH668 |
| C | HOH673 |
| C | GLY13 |
| C | VAL14 |
| C | ALA15 |
| C | SER19 |
| C | ILE20 |
| C | GLN40 |
| C | LEU44 |
| C | CYS63 |
| C | ASP64 |
| C | VAL65 |
| C | SER91 |
| C | ILE92 |
| C | GLY93 |
| C | LEU144 |
| C | SER145 |
| C | LYS163 |
| C | ALA189 |
| C | GLY190 |
| C | PRO191 |
| C | ILE192 |
| C | THR194 |
| C | ALA196 |
| C | TCL603 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TCL C 603 |
| Chain | Residue |
| C | GLY93 |
| C | ALA95 |
| C | LEU100 |
| C | TYR146 |
| C | TYR156 |
| C | ALA196 |
| C | ILE200 |
| C | NAD503 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD D 504 |
| Chain | Residue |
| D | GLY13 |
| D | VAL14 |
| D | ALA15 |
| D | SER19 |
| D | ILE20 |
| D | GLN40 |
| D | LEU44 |
| D | CYS63 |
| D | ASP64 |
| D | VAL65 |
| D | SER91 |
| D | ILE92 |
| D | GLY93 |
| D | LEU144 |
| D | SER145 |
| D | LYS163 |
| D | ALA189 |
| D | GLY190 |
| D | PRO191 |
| D | ILE192 |
| D | THR194 |
| D | ALA196 |
| D | TCL604 |
| D | HOH618 |
| D | HOH621 |
| D | HOH627 |
| D | HOH629 |
| D | HOH659 |
| D | HOH672 |
| D | HOH677 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TCL D 604 |
| Chain | Residue |
| D | GLY93 |
| D | ALA95 |
| D | LEU100 |
| D | TYR146 |
| D | TYR156 |
| D | ALA196 |
| D | ILE200 |
| D | NAD504 |
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 | 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 |
