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Structure of threonine synthase from arabidopsis thaliana

Analyse Structure of threonine synthase from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E5X
Type: protein
Length: 884 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Threonine synthase
EC: 4.2.99.2
UniProt: Q39144
Pockets: 11 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Threonine synthase (EC 4.2.99.2)	protein	451	43% helix, 15% strand	Q39144
B	Threonine synthase (EC 4.2.99.2)	protein	433	44% helix, 15% strand	Q39144

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	744	0.83	0.87	136	empty
2	613	0.66	0.76	83	empty
3	181	0.57	0.80	19	empty
4	185	0.55	0.79	20	empty
5	104	0.48	0.81	23	empty

Interfaces

1 interface between chains.

A–B · 4228 Å² buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 26 modified (engineered, nonstandard).

Compared structures

1E5X · Structure of threonine synthase from Arabidopsis thaliana · 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 Q39144
Elsewhere: RCSB PDB 1E5X · PDBe 1E5X · UniProt Q39144

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