Structure of PDB 2ntv Chain B

Receptor sequence
>2ntvB (length=268) Species: 1769 (Mycobacterium leprae) [Search protein sequence]
AGLLEGKRILVSGIITDSSIAFHIAKVAQEAGAQLVLTGFDRLRLIQRIA
DRLPDKAPLIELDVQNEEHLATLAERVTAEIGEGNKLDGVVHSIGFMPQT
GMGTNQFFDAPYEDVSKGIHISTYSYASLAKALLLIMNSGGSIVGMDFDP
TRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSA
IVGGAFGEEAGAQMQLLEEGWDQRAPIGWNMKDPTPVAKTVCALLSEWLP
ATTGSIIYADGGASTQLL
3D structure
PDB2ntv Mechanism of thioamide drug action against tuberculosis and leprosy.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y158 K165
Catalytic site (residue number reindexed from 1) Y157 K164
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 P1H B G14 I16 S20 I21 F41 S94 I95 G96 I122 M147 D148 F149 Y158 K165 A191 G192 P193 I194 T196 A198 M199 L218 W222 G13 I15 S19 I20 F40 S93 I94 G95 I121 M146 D147 F148 Y157 K164 A190 G191 P192 I193 T195 A197 M198 L217 W221 MOAD: Ki=11nM
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
GO:0050343 trans-2-enoyl-CoA reductase (NADH) 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:2ntv, PDBe:2ntv, PDBj:2ntv
PDBsum2ntv
PubMed17227913
UniProtQ9CBM1

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