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X-ray structure of enoyl-acyl carrier protein reductase from bacillus anthracis with C-terminal his tag (apo form)

Analyse X-ray structure of enoyl-acyl carrier protein reductase from bacillus anthracis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YCX
Type: protein
Length: 229 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-[acyl-carrier-protein] reductase [NADH] fabi
EC: 1.3.1.9
UniProt: Q81GI3
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-[acyl-carrier-protein] reductase [NADH] fabi (EC 1.3.1.9)	protein	229	46% helix, 17% strand	Q81GI3

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	119	0.53	0.82	20	empty
2	101	0.39	0.76	21	empty

Compared structures

5YCX · X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with… · the same entry in another collection · chain A against A, TM-score 1.00
Q81GI3 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH] fabi… · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q81GI3
Elsewhere: RCSB PDB 5YCX · PDBe 5YCX · UniProt Q81GI3

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