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Structure of PDB 5ycs Chain C Binding Site BS02

Receptor Information >5ycs Chain C (length=256) Species: 226900 (Bacillus cereus ATCC 14579) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] MELLQGKTFVVMGVANQRSIAWGIARSLHNAGAKLIFTYAGERLERNVRE LADTLEGQESLVLPCDVTNDEELTACFETIKQEVGTIHGVAHCIAFANRD DLKGEFVDTSRDGFLLAQNISAFSLTAVAREAKKVMTEGGNILTLTYLGG ERVVKNYNVMGVAKASLEASVKYLANDLGQHGIRVNAISAGPIRTLSAKG VGDFNSILREIEERAPLRRTTTQEEVGDTAVFLFSDLARGVTGENIHVDS GYHILG

Ligand information Ligand ID TCL InChI InChI=1S/C12H7Cl3O2/c13-7-1-3-11(9(15)5-7)17-12-4-2-8(14)6-10(12)16/h1-6,16H InChIKey XEFQLINVKFYRCS-UHFFFAOYSA-N SMILES Software SMILES ACDLabs 10.04 Clc2cc(Cl)ccc2Oc1ccc(Cl)cc1O OpenEye OEToolkits 1.5.0 c1cc(c(cc1Cl)O)Oc2ccc(cc2Cl)Cl CACTVS 3.341 Oc1cc(Cl)ccc1Oc2ccc(Cl)cc2Cl Formula C12 H7 Cl3 O2 Name TRICLOSAN ChEMBL CHEMBL849 DrugBank DB08604 ZINC ZINC000000002216 PDB chain 5ycs Chain C Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 5ycs Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis Resolution 1.95 Å Binding residue (original residue number in PDB) A95 A97 Y147 Y157 M160 S197 Binding residue (residue number reindexed from 1) A95 A97 Y147 Y157 M160 S197 Annotation score 1

Enzymatic activity Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).

Gene Ontology Molecular Function GO:0000166 nucleotide binding GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity GO:0016491 oxidoreductase activity GO:0036094 small molecule binding GO:0042802 identical protein binding GO:0070401 NADP+ binding GO:0141148 enoyl-[acyl-carrier-protein] reductase (NADPH) activity

	Biological Process
GO:0006633	fatty acid biosynthetic process
GO:0030497	fatty acid elongation

	Cellular Component
GO:1902494	catalytic complex

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