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Crystal structure of B. pseudomallei FabI in complex with NAD and PT412

Analyse Crystal structure of B. pseudomallei FabI in complex with NAD and PT412 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I9N
Type: protein
Length: 261 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.512
Source: Burkholderia pseudomallei
Molecule: Enoyl-[acyl-carrier-protein] reductase [NADH]
EC: 1.3.1.9
UniProt: A0A069B9A4
Ligands: NAD, 69J
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · resolution 2.512 · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9)	protein	261	47% helix, 16% strand	A0A069B9A4

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
69J · 5-ethyl-4-fluoro-2-(2-nitrophenoxy)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	559	0.81	0.86	48	NAD, 69J
2	79	0.40	0.78	20	empty

Compared structures

5I9N · Crystal structure of B. pseudomallei fabi in complex with NAD and PT412 · 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 A0A069B9A4
Elsewhere: RCSB PDB 5I9N · PDBe 5I9N · UniProt A0A069B9A4

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