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Crystal structure of trehalose synthase tret from P. horikoshi

Analyse Crystal structure of trehalose synthase tret from P. horikoshi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X6Q
Type: protein
Length: 817 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Trehalose-synthase tret
UniProt: O58762
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trehalose-synthase tret	protein	408	48% helix, 15% strand	O58762
B	Trehalose-synthase tret	protein	409	48% helix, 15% strand	O58762

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	912	0.75	0.78	76	empty
2	1070	0.74	0.77	70	empty
3	1020	0.73	0.76	69	empty
4	59	0.30	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 304 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

2X6Q · Crystal structure of trehalose synthase TreT from P.horikoshi · the same entry in another collection · chain A against A, TM-score 1.00
O58762 · AlphaFold monomer V2.0 prediction for trehalose synthase (O58762) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O58762
Elsewhere: RCSB PDB 2X6Q · PDBe 2X6Q · UniProt O58762

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