Structure of PDB 5cpf Chain C

Receptor sequence
>5cpfC (length=267) Species: 83331 (Mycobacterium tuberculosis CDC1551) [Search protein sequence]
GLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITD
RLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTG
MGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPS
RAMPAYNWMTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAI
VGGALGEEAGAQAQLLEEGWDQRAPIGWNMKDATPVAKTVCALLSDWLPA
TTGDIIYADGGAHTQLL
3D structure
PDB5cpf Rational Modulation of the Induced-Fit Conformational Change for Slow-Onset Inhibition in Mycobacterium tuberculosis InhA.
ChainC
Resolution3.409 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) Y156 K163
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 C G14 I15 I16 S20 I21 F41 D64 V65 S94 I95 G96 I122 M147 D148 K165 A191 P193 I194 T196 G12 I13 I14 S18 I19 F39 D62 V63 S92 I93 G94 I120 M145 D146 K163 A189 P191 I192 T194
BS02 53K C G96 F97 F149 A157 Y158 L218 G94 F95 F147 A155 Y156 L216
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
GO:0046677 response to antibiotic

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Molecular Function
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Biological Process
External links
PDB RCSB:5cpf, PDBe:5cpf, PDBj:5cpf
PDBsum5cpf
PubMed26147157
UniProtP9WGR0|INHA_MYCTO Enoyl-[acyl-carrier-protein] reductase [NADH] (Gene Name=inhA)

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