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Crystal structure of InhA bound to triclosan derivative

Analyse Crystal structure of InhA bound to triclosan derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FNH
Type: protein
Length: 268 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.8
Source: Mycobacterium tuberculosis
Molecule: Enoyl-[acyl-carrier-protein] reductase [NADH]
EC: 1.3.1.9
UniProt: P0A5Y6
Ligands: NAD, JPJ
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.8 · 1 distinct chain · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	268	47% helix, 14% strand	P0A5Y6

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
JPJ · 2-(2,4-dichlorophenoxy)-5-(2-phenylethyl)phenol · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	578	0.83	0.87	47	NAD, JPJ
2	111	0.46	0.79	20	empty

Compared structures

3FNH · Crystal structure of inha bound to triclosan derivative · the same entry in another collection · chain A against A, TM-score 1.00

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 P0A5Y6
Elsewhere: RCSB PDB 3FNH · PDBe 3FNH · UniProt P0A5Y6

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