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Apo form of threonine synthase from thermus thermophilus HB8

Analyse Apo form of threonine synthase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AEY
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: Q5SL02
Ligands: SO4
Pockets: 4 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Threonine synthase (EC 4.2.3.1)	protein	350	47% helix, 17% strand	Q5SL02
B	Threonine synthase (EC 4.2.3.1)	protein	348	47% helix, 17% strand	Q5SL02

Ligands and binding sites

SO4 · Sulfate ion · ion · 8 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	617	0.73	0.80	73	SO4
2	591	0.73	0.80	67	SO4
3	148	0.53	0.80	22	empty
4	82	0.32	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 3361 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

3AEY · Apo form of threonine synthase from Thermus thermophilus HB8 · 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 Q5SL02
Elsewhere: RCSB PDB 3AEY · PDBe 3AEY · UniProt Q5SL02

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