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L-threonine dehydrogenase from trypanosoma brucei.

Analyse L-threonine dehydrogenase from trypanosoma brucei. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L9A
Type: protein
Length: 641 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-threonine 3-dehydrogenase
EC: 1.1.1.103
UniProt: Q7YW97
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-threonine 3-dehydrogenase (EC 1.1.1.103)	protein	321	46% helix, 15% strand	Q7YW97
B	L-threonine 3-dehydrogenase (EC 1.1.1.103)	protein	320	46% helix, 15% strand	Q7YW97

Ligands and binding sites

ACT · Acetate ion · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	1180	0.81	0.82	87	ACT
2	516	0.72	0.81	52	ACT
3	525	0.66	0.77	53	empty
4	64	0.31	0.75	13	empty

Interfaces

1 interface between chains.

A–B · 521 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5L9A · L-threonine dehydrogenase from trypanosoma brucei. · 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 Q7YW97
Elsewhere: RCSB PDB 5L9A · PDBe 5L9A · UniProt Q7YW97

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