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The crystal structure of toxoplasma gondii enoyl acyl carrier protein reductase

Analyse The crystal structure of toxoplasma gondii enoyl acyl carrier protein reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O50
Type: protein
Length: 580 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-acyl carrier reductase
EC: 1.3.1.9
UniProt: Q6UCJ9
Pockets: 9 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-acyl carrier reductase (EC 1.3.1.9)	protein	290	46% helix, 17% strand	Q6UCJ9
B	Enoyl-acyl carrier reductase (EC 1.3.1.9)	protein	290	44% helix, 17% strand	Q6UCJ9

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	482	0.65	0.77	42	empty
2	444	0.64	0.77	40	empty
3	218	0.52	0.77	21	empty
4	138	0.48	0.78	24	empty
5	117	0.45	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 1549 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

2O50 · The crystal structure of Toxoplasma gondii Enoyl acyl carrier protein reductase · 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 Q6UCJ9
Elsewhere: RCSB PDB 2O50 · PDBe 2O50 · UniProt Q6UCJ9

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