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Crystal structure of an udp-forming alpha, alpha-terhalose-phosphate synthase from burkholderia xenovorans

Analyse Crystal structure of an udp-forming alpha, alpha-terhalose-phosphate synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HXA
Type: protein
Length: 448 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA,ALPHA-trehalose-phosphate synthase (udp-forming)
EC: 2.4.1.15
UniProt: Q142X8
Ligands: NA
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA,ALPHA-trehalose-phosphate synthase (udp-forming) (EC 2.4.1.15)	protein	448	47% helix, 19% strand	Q142X8

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 10 copies · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	856	0.73	0.77	69	empty
2	65	0.38	0.79	18	NA
3	52	0.35	0.78	13	empty

Compared structures

5HXA · Crystal structure of an UDP-forming alpha, alpha-terhalose-phosphate synthase from… · 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 Q142X8
Elsewhere: RCSB PDB 5HXA · PDBe 5HXA · UniProt Q142X8

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