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Mycobacterium leprae inha bound with pth-NAD adduct

Analyse Mycobacterium leprae inha bound with pth-NAD adduct in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NTV
Type: protein
Length: 536 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-[acp] reductase
UniProt: Q9CBM1
Ligands: P1H
Pockets: 2 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Enoyl-[acp] reductase	protein	268	46% helix, 16% strand	Q9CBM1

Ligands and binding sites

P1H · {(2R,3S,4R,5R)-5-[(4S)-3-(aminocarbonyl)-4-(2-propylisonicotinoyl)pyridin-1(4H)-yl]-3,4-dihydroxytetrahydrofuran-2-yl}m ethyl [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	781	0.80	0.83	64	P1H
2	1030	0.79	0.80	90	P1H

Interfaces

1 interface between chains.

A–B · 1397 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2NTV · Mycobacterium leprae InhA bound with PTH-NAD adduct · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9CBM1
Elsewhere: RCSB PDB 2NTV · PDBe 2NTV · UniProt Q9CBM1

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