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Crystal structure of B. pseudomallei fabi in complex with NAD and PT12

Analyse Crystal structure of B. pseudomallei fabi in complex with NAD and PT12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I8Z
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-[acyl-carrier-protein] reductase [NADH]
EC: 1.3.1.9
UniProt: A0A069B9A4
Ligands: NAD, JA1
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 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	257	47% helix, 16% strand	A0A069B9A4

Ligands and binding sites

NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
JA1 · 5-hexyl-2-(4-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	616	0.79	0.84	53	NAD, JA1
2	55	0.29	0.74	13	empty

Compared structures

5I8Z · Crystal structure of B. pseudomallei FabI in complex with NAD and PT12 · 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 5I8Z · PDBe 5I8Z · UniProt A0A069B9A4

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