5CPF: Enoyl-[acyl-carrier-protein] reductase [NADH]

Compensation of the effect of isoleucine to alanine mutation by designed inhibition in the InhA enzyme. Determined by X-ray diffraction at 3.41 Å resolution. Released 12 Aug 2015.

Method
X-ray diffraction
Resolution
3.41 Å
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Chains
4
Atoms
8,002
Mol. weight
126.82 kDa
Ligands
53K, NAD
Released
12 Aug 2015

Explore 5CPF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CPF contains 54 α-helices and 38 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand9-1241
α-helix21-3111
β-strand35-4061
α-helix44-518
β-strand60-6231
α-helix68-8215
β-strand88-9361
α-helix113-1208
α-helix121-1255
α-helix126-1349
α-helix135-1373
β-strand138-148111
β-strand15412
α-helix159-18123
β-strand185-19171
α-helix198-2025
α-helix209-22517
α-helix236-24611
β-strand257-26041
β-strand26713
Chain B: 15 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand7-1264
α-helix21-3111
β-strand34-4074
α-helix44-518
β-strand60-6234
α-helix68-8215
β-strand88-9364
α-helix100-1023
α-helix108-1103
α-helix113-1208
α-helix121-1255
α-helix126-1349
α-helix135-1373
β-strand138-148114
β-strand15415
α-helix159-18123
β-strand185-19174
α-helix197-2059
α-helix208-2114
α-helix213-2164
α-helix220-2245
α-helix236-24611
β-strand256-26054
β-strand26716
Chain C: 13 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand9-1247
α-helix21-3111
α-helix341
β-strand35-4067
α-helix44-518
β-strand60-6237
α-helix68-8215
β-strand8818
β-strand91-9337
α-helix113-1208
α-helix121-1255
α-helix126-1349
α-helix135-1373
β-strand13818
β-strand143-14867
β-strand15413
α-helix159-18224
β-strand185-19177
α-helix199-2024
α-helix209-22517
α-helix236-24611
β-strand256-26057
α-helix264-2663
β-strand26712
Chain D: 15 helices, 9 β-strands
ElementResiduesLengthSheet
β-strand9-1359
α-helix21-3111
β-strand35-4069
α-helix44-518
β-strand60-6239
α-helix68-8215
β-strand88-9369
α-helix100-1023
α-helix108-1103
α-helix113-12311
α-helix126-1349
α-helix135-1373
β-strand138-148119
β-strand15416
α-helix159-17820
β-strand185-19179
α-helix197-1982
α-helix199-2035
α-helix208-2103
α-helix213-22311
α-helix236-24611
β-strand257-26049
α-helix264-2663
β-strand26715

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Enoyl-[acyl-carrier-protein] reductase [NADH]A, B, C, Dprotein289Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)P9WGR0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>5CPF_1 Enoyl-[acyl-carrier-protein] reductase [NADH] (chains A, B, C, D)
MGSSHHHHHHSSGLVPRGSHMTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTG
FDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQ
TGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNW
MTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQAQLLEE
GWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL

Ligands and cofactors

IDNameFormulaCopies
53K2-(2-methylphenoxy)-5-[(4-phenyl-1H-1,2,3-triazol-1-yl)methyl]phenolC22 H19 N3 O24
NADNicotinamide-adenine-dinucleotideC21 H27 N7 O14 P24

Primary citation

Rational Modulation of the Induced-Fit Conformational Change for Slow-Onset Inhibition in Mycobacterium tuberculosis InhA. Lai, C.T., Li, H.J., Yu, W. et al. Biochemistry (2015) 54:4683-4691. DOI 10.1021/acs.biochem.5b00284 · PubMed

Other PDB entries of the same protein (UniProt P9WGR0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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