1C14
CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 501 |
Chain | Residue |
A | GLY13 |
A | VAL65 |
A | SER91 |
A | ILE92 |
A | GLY93 |
A | ILE119 |
A | LEU144 |
A | SER145 |
A | LYS163 |
A | ALA189 |
A | GLY190 |
A | VAL14 |
A | PRO191 |
A | ILE192 |
A | THR194 |
A | LEU195 |
A | ALA196 |
A | TCL502 |
A | HOH2006 |
A | HOH2025 |
A | HOH2086 |
A | ALA15 |
A | SER19 |
A | ILE20 |
A | GLN40 |
A | LEU44 |
A | CYS63 |
A | ASP64 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TCL A 502 |
Chain | Residue |
A | GLY93 |
A | ALA95 |
A | LEU100 |
A | TYR146 |
A | TYR156 |
A | ALA196 |
A | ALA197 |
A | ILE200 |
A | PHE203 |
A | NAD501 |
site_id | AC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 1501 |
Chain | Residue |
B | GLY1013 |
B | ALA1015 |
B | SER1019 |
B | ILE1020 |
B | GLN1040 |
B | LEU1044 |
B | CYS1063 |
B | ASP1064 |
B | VAL1065 |
B | SER1091 |
B | ILE1092 |
B | GLY1093 |
B | LEU1144 |
B | SER1145 |
B | LYS1163 |
B | ALA1189 |
B | GLY1190 |
B | PRO1191 |
B | ILE1192 |
B | THR1194 |
B | LEU1195 |
B | ALA1196 |
B | TCL1502 |
B | HOH2005 |
B | HOH2041 |
B | HOH2048 |
B | HOH2063 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TCL B 1502 |
Chain | Residue |
B | GLY1093 |
B | ALA1095 |
B | TYR1146 |
B | TYR1156 |
B | ALA1196 |
B | ALA1197 |
B | ILE1200 |
B | PHE1203 |
B | MET1206 |
B | NAD1501 |
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 | TYR1146 | |
B | TYR1156 |
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 | GLN1040 | |
B | ASP1064 | |
B | ILE1092 | |
B | LYS1163 | |
B | ILE1192 | |
A | SER19 | |
A | GLN40 | |
A | ASP64 | |
A | ILE92 | |
A | LYS163 | |
A | ILE192 | |
B | GLY1013 | |
B | SER1019 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ALA95 | |
B | ALA1095 |
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 | LYS1201 | |
B | ARG1204 | |
B | LYS1205 |
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 | GLU1150 |
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 | LYS1163 | |
B | TYR1156 |
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 | LYS1163 | |
B | MET1159 |
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 | TYR1156 | proton acceptor, proton donor |
B | LYS1163 | electrostatic stabiliser |