Crystal structure of the inha from mycobacterium tuberculosis in complex with AN12855, ebsi 4333.

Structure

x-ray diffraction · 4 distinct chains · 45% helix, 16% strand (DSSP).

Ligands and binding sites

• 9JM · [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonylpyridin-1-ium-1-yl)-4-[[5-[4-cyano-2-[(~{E})-hydroxyiminomethyl]phenoxy]-1-oxidanyl-3~{H}-2, 1$L^{4}-benzoxaborol-1-yl]oxy]-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R}, 5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate · ligand · 6 copies · chains A, B, C, D, E, F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

17 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Interfaces

9 interfaces between chains.

• D–F · 1551 Ų buried · 19 hydrogen bonds · protein-protein
• C–E · 1529 Ų buried · 20 hydrogen bonds · protein-protein
• E–F · 1466 Ų buried · 18 hydrogen bonds · protein-protein
• A–B · 1465 Ų buried · 20 hydrogen bonds · protein-protein
• C–D · 1462 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

• 5VRN · Crystal structure of the inha from mycobacterium tuberculosis in complex with AN12855… · the same entry in another collection · chain F against F, TM-score 1.00
• P9WGR0 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain D against A, TM-score 0.99

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P9WGR0
• Elsewhere: RCSB PDB 5VRN · PDBe 5VRN · UniProt P9WGR0