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

Structure

x-ray diffraction · resolution 2.5 · 4 distinct chains · 45% helix, 17% strand (DSSP).

Ligands and binding sites

• 9JJ · [[(2~{R},3~{S},4~{R},5~{R})-5-(3-aminocarbonylpyridin-1-ium-1-yl)-3-oxidanyl-4-[[1-oxidanyl-6-[4-(trifluoromethyl)phenoxy]-3~{H}-2,1$l^{4}-benzoxaborol-1-yl]oxy]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 · 4 copies · chains A, B, C, D

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–B · 1554 Ų buried · 16 hydrogen bonds · protein-protein
• C–D · 1550 Ų buried · 16 hydrogen bonds · protein-protein
• B–C · 1476 Ų buried · 17 hydrogen bonds · protein-protein
• A–D · 1463 Ų buried · 17 hydrogen bonds · protein-protein
• A–C · 690 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

• 5VRM · Crystal structure of the inha from mycobacterium tuberculosis in complex with AN12855… · the same entry in another collection · chain D against D, 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 C 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 5VRM · PDBe 5VRM · UniProt P9WGR0