5MTP: M. tuberculosis InhA inhibited by PT514
Crystal structure of M. tuberculosis InhA inhibited by PT514. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Feb 2017.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- Mycobacterium tuberculosis CDC1551
- Chains
- 8
- Atoms
- 17,867
- Mol. weight
- 254.12 kDa
- Ligands
- NAD, 53K
- Released
- 15 Feb 2017
Explore 5MTP in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5MTP contains 145 α-helices and 72 β-strands across 8 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: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 1 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 1 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 1 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 1 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 1 |
| β-strand | 154 | 1 | 2 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 1 |
| α-helix | 192-193 | 2 | |
| α-helix | 197 | 1 | |
| α-helix | 198-204 | 7 | |
| α-helix | 205-207 | 3 | |
| α-helix | 208-210 | 3 | |
| α-helix | 211-218 | 8 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 1 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 3 |
Chains B, D and F: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 4 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 4 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 4 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 4 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 4 |
| β-strand | 154 | 1 | 5 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 4 |
| α-helix | 192-193 | 2 | |
| α-helix | 197-202 | 6 | |
| α-helix | 211-218 | 8 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 4 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 6 |
Chain C: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 9 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 9 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 9 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 9 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 9 |
| β-strand | 154 | 1 | 10 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 9 |
| α-helix | 192-193 | 2 | |
| α-helix | 197 | 1 | |
| α-helix | 198-203 | 6 | |
| α-helix | 204-206 | 3 | |
| α-helix | 208-213 | 6 | |
| α-helix | 214-218 | 5 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 9 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 11 |
Chain E: 20 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 7 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 7 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 7 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 7 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 7 |
| β-strand | 154 | 1 | 3 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 7 |
| α-helix | 192-193 | 2 | |
| α-helix | 197 | 1 | |
| α-helix | 198-204 | 7 | |
| α-helix | 205-206 | 2 | |
| α-helix | 208-210 | 3 | |
| α-helix | 211-218 | 8 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 7 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 2 |
Chain G: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 8 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 8 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 8 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 8 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 8 |
| β-strand | 154 | 1 | 6 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 8 |
| α-helix | 192-193 | 2 | |
| α-helix | 197-203 | 7 | |
| α-helix | 212-218 | 7 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 8 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 5 |
Chain H: 17 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 16 |
| α-helix | 21-31 | 11 | |
| α-helix | 34 | 1 | |
| β-strand | 35-40 | 6 | 16 |
| α-helix | 44-51 | 8 | |
| β-strand | 60-62 | 3 | 16 |
| α-helix | 68-82 | 15 | |
| β-strand | 88-93 | 6 | 16 |
| α-helix | 100-102 | 3 | |
| α-helix | 108-110 | 3 | |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-134 | 9 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138-148 | 11 | 16 |
| β-strand | 154 | 1 | 14 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 16 |
| α-helix | 192-193 | 2 | |
| α-helix | 197-202 | 6 | |
| α-helix | 212-218 | 7 | |
| α-helix | 219-223 | 5 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 16 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 13 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Enoyl-[acyl-carrier-protein] reductase [NADH] | A, B, C, D, E, F, G, H | protein | 289 | Mycobacterium tuberculosis CDC1551 | P9WGR0 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>5MTP_1 Enoyl-[acyl-carrier-protein] reductase [NADH] (chains A, B, C, D, E, F, G, H)
MGSSHHHHHHSSGLVPRGSHMTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTG
FDRLRLIQRITDRLPAKAPLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQ
TGMGINPFFDAPYADVSKGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNW
MTVAKSALESVNRFVAREAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEE
GWDQRAPIGWNMKDATPVAKTVCALLSDWLPATTGDIIYADGGAHTQLL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAD | Nicotinamide-adenine-dinucleotide | C21 H27 N7 O14 P2 | 8 |
| 53K | 2-(2-methylphenoxy)-5-[(4-phenyl-1H-1,2,3-triazol-1-yl)methyl]phenol | C22 H19 N3 O2 | 8 |
Water and common crystallization additives (CL, NA) are not listed.
Primary citation
Evaluating the Contribution of Transition-State Destabilization to Changes in the Residence Time of Triazole-Based InhA Inhibitors. Spagnuolo, L.A., Eltschkner, S., Yu, W. et al. J Am Chem Soc (2017) 139:3417-3429. DOI 10.1021/jacs.6b11148 · PubMed
Other PDB entries of the same protein (UniProt P9WGR0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4TRJ 1.73 Å, Crystal structure of Mycobacterium tuberculosis enoyl reductase (INHA) complexed with…
- 5CPF 3.41 Å, Compensation of the effect of isoleucine to alanine mutation by designed inhibition in…
Browse structure collections
About this viewer
MolViewer shows 5MTP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.