Structure of Mycobacterium tuberculosis InhA in complex with pyridomycin derivative KV41a (compound 11). Determined by X-ray diffraction at 1.66 Å resolution. Released 11 Feb 2026.
Explore 9RJK in 3D Show helices and sheets RCSB PDB PDBe
9RJK contains 55 α-helices and 36 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 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 | 211-225 | 15 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 1 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 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 | 212-225 | 14 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 4 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 7 |
| α-helix | 21-31 | 11 | |
| 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 | 6 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 7 |
| α-helix | 197-203 | 7 | |
| α-helix | 210-225 | 16 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 7 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 8 |
| α-helix | 22-31 | 10 | |
| β-strand | 35-40 | 6 | 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 | 3 |
| α-helix | 159-180 | 22 | |
| β-strand | 185-191 | 7 | 8 |
| α-helix | 197-204 | 8 | |
| α-helix | 209-225 | 17 | |
| α-helix | 236-246 | 11 | |
| β-strand | 256-260 | 5 | 8 |
| α-helix | 264-266 | 3 | |
| β-strand | 267 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Enoyl-[acyl-carrier-protein] reductase [NADH] | A, B, C, D | protein | 272 | Mycobacterium tuberculosis | P9WGR1 (AlphaFold model) |
>9RJK_1 Enoyl-[acyl-carrier-protein] reductase [NADH] (chains A, B, C, D) GSHMTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAK APLLELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVS KGIHISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAR EAGKYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATP VAKTVCALLSDWLPATTGDIIYADGGAHTQLL
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1JG3 | ~{N}-[(2~{Z},5~{R},6~{S},9~{S},10~{S},11~{R})-2-butan-2-ylidene-5,11-dimethyl-1… | C28 H32 F N3 O8 | 4 |
Water and common crystallization additives (PEG) are not listed.
Optimizing the Antibiotic Potency and Metabolic Stability of Pyridomycin Using a Semisynthetic Approach. Valderrama, K., Horlacher, O., Publicola, G. et al. J Med Chem (2026) 69:2496-2508. DOI 10.1021/acs.jmedchem.5c02409 · PubMed
Other PDB entries of the same protein (UniProt P9WGR1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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