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Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase catalysing the production of large cyclic glucans

Analyse Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CWY
Type: protein
Length: 500 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amylomaltase
EC: 2.4.1.25
UniProt: O87172
Pockets: 8 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amylomaltase (EC 2.4.1.25)	protein	500	46% helix, 13% strand	O87172

Pockets

8 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	108	0.79	0.98	28	empty
2	620	0.68	0.77	49	empty
3	140	0.47	0.77	26	empty
4	80	0.39	0.78	18	empty
5	56	0.38	0.79	12	empty

Compared structures

1CWY · Crystal structure of amylomaltase from thermus aquaticus, a glycosyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
O87172 · AlphaFold monomer V2.0 prediction for 4-alpha-glucanotransferase (O87172) · a predicted model of the same protein · 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 O87172
Elsewhere: RCSB PDB 1CWY · PDBe 1CWY · UniProt O87172

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