Research workbench

Crystal structure of B. pseudomallei fabi in complex with NAD and PT01

Analyse Crystal structure of B. pseudomallei fabi in complex with NAD and PT01 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I7S
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, E9P
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
E9P · 5-ethyl-2-phenoxyphenol · 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	484	0.79	0.86	44	NAD, E9P
2	79	0.36	0.76	17	empty

Compared structures

5I7S · Crystal structure of B. pseudomallei FabI in complex with NAD and PT01 · 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 5I7S · PDBe 5I7S · UniProt A0A069B9A4

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.