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Structure of mycobacterium tuberculosis threonine synthase

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

PDB: 2D1F
Type: protein
Length: 698 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Threonine synthase
EC: 4.2.3.1
UniProt: P66902
Ligands: PLP
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Threonine synthase (EC 4.2.3.1)	protein	349	47% helix, 16% strand	P66902

Ligands and binding sites

PLP · Pyridoxal-5'-phosphate · ligand · 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	655	0.77	0.82	68	PLP
2	633	0.76	0.82	75	PLP
3	356	0.73	0.85	55	empty
4	61	0.33	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 3227 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

2D1F · Structure of Mycobacterium tuberculosis threonine synthase · 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 P66902
Elsewhere: RCSB PDB 2D1F · PDBe 2D1F · UniProt P66902

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