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Crystal structure of glucodextranase complexed with acarbose

Analyse Crystal structure of glucodextranase complexed with acarbose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ULV
Type: protein
Length: 1,019 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glucodextranase
EC: 3.2.1.70
UniProt: Q9LBQ9
Ligands: AC1, GLC, CA
Pockets: 7 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glucodextranase (EC 3.2.1.70)	protein	1019	26% helix, 29% strand	Q9LBQ9

Ligands and binding sites

AC1 · 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose · ligand · chains A
GLC · alpha-D-glucopyranose · sugar · chains A
CA · Calcium ion · metal · 6 copies · chains A

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

Pockets

7 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	220	0.59	0.80	27	GLC, AC1
2	180	0.47	0.76	28	empty
3	127	0.47	0.78	20	empty
4	57	0.42	0.82	17	empty
5	84	0.38	0.78	21	empty

Compared structures

1ULV · Crystal Structure of Glucodextranase Complexed with Acarbose · 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 Q9LBQ9
Elsewhere: RCSB PDB 1ULV · PDBe 1ULV · UniProt Q9LBQ9

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