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Crystal structure of amylosucrase from deinococcus geothermalis

Analyse Crystal structure of amylosucrase from deinococcus geothermalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UCQ
Type: protein
Length: 651 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amylosucrase
EC: 2.4.1.4
UniProt: Q1J0W0
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amylosucrase (EC 2.4.1.4)	protein	651	46% helix, 16% strand	Q1J0W0

Ligands and binding sites

GOL · Glycerol · additive · 13 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	517	0.77	0.84	67	TRS, GOL
2	173	0.50	0.78	20	empty
3	111	0.49	0.81	25	GOL
4	142	0.48	0.78	29	empty
5	57	0.30	0.75	12	empty

Compared structures

3UCQ · Crystal structure of amylosucrase from Deinococcus geothermalis · 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 Q1J0W0
Elsewhere: RCSB PDB 3UCQ · PDBe 3UCQ · UniProt Q1J0W0

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