Structure of PDB 5ugs Chain D

Receptor sequence
>5ugsD (length=268) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
TGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRIT
DRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQT
GMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDP
SRAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSA
IVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLP
ATTGDIIYADGGAHTQLL
3D structure
PDB5ugs Evaluating the Contribution of Transition-State Destabilization to Changes in the Residence Time of Triazole-Based InhA Inhibitors.
ChainD
Resolution2.8 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 NAD D G14 I15 I16 S20 I21 F41 D64 V65 S94 I95 G96 M147 D148 F149 K165 A191 P193 I194 T196 A198 G13 I14 I15 S19 I20 F40 D63 V64 S93 I94 G95 M146 D147 F148 K164 A190 P192 I193 T195 A197
BS02 XT5 D G96 F97 F149 Y158 A198 M199 V203 G95 F96 F148 Y157 A197 M198 V202
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0005504 fatty acid binding
GO:0016491 oxidoreductase activity
GO:0050343 trans-2-enoyl-CoA reductase (NADH) activity
GO:0070403 NAD+ binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation
GO:0046677 response to antibiotic
GO:0071768 mycolic acid biosynthetic process
Cellular Component
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Cellular Component
External links
PDB RCSB:5ugs, PDBe:5ugs, PDBj:5ugs
PDBsum5ugs
PubMed28151657
UniProtP9WGR1|INHA_MYCTU Enoyl-[acyl-carrier-protein] reductase [NADH] (Gene Name=inhA)

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