Structure of PDB 2qio Chain B

Receptor sequence
>2qioB (length=256) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MELLQGKTFVVMGVANQRSIAWGIARSLHNAGAKLIFTYAGERLERNVRE
LADTLEGQESLVLPCDVTNDEELTACFETIKQEVGTIHGVAHCIAFANRD
DLKGEFVDTSRDGFLLAQNISAFSLTAVAREAKKVMTEGGNILTLTYLGG
ERVVKNYNVMGVAKASLEASVKYLANDLGQHGIRVNAISAGPIRTLSAKG
VGDFNSILREIEERAPLRRTTTQEEVGDTAVFLFSDLARGVTGENIHVDS
GYHILG
3D structure
PDB2qio Design and synthesis of aryl ether inhibitors of the Bacillus anthracis enoyl-ACP reductase.
ChainB
Resolution2.44 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S19 Y147 Y157 M160 K164 K199
Catalytic site (residue number reindexed from 1) S19 Y147 Y157 M160 K164 K199
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAD B G13 V14 A15 S19 I20 A40 D66 V67 C93 I94 A95 L145 T146 Y147 K164 A190 P192 I193 T195 S197 G13 V14 A15 S19 I20 A40 D66 V67 C93 I94 A95 L145 T146 Y147 K164 A190 P192 I193 T195 S197
BS02 TCL B A95 A97 L102 Y147 Y157 M160 S197 A95 A97 L102 Y147 Y157 M160 S197 MOAD: ic50=3.6uM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2qio, PDBe:2qio, PDBj:2qio
PDBsum2qio
PubMed18663709
UniProtA0A6L8PBX8

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