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Crystal structure of barley limit dextrinase co-crystallized with 25MM maltotetraose

Analyse Crystal structure of barley limit dextrinase co-crystallized with 25MM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J3T
Type: protein
Length: 870 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Limit dextrinase
EC: 3.2.1.41
UniProt: Q9FYY0
Ligands: GLC, CA, IOD, CL
Pockets: 7 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Limit dextrinase (EC 3.2.1.41)	protein	870	32% helix, 23% strand	Q9FYY0

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 5 copies · chains A
CA · Calcium ion · metal · chains A
IOD · Iodide ion · ion · 9 copies · chains A
CL · Chloride ion · ion · 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, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	150	0.70	0.89	35	IOD
2	439	0.68	0.80	59	GLC
3	109	0.56	0.84	22	IOD
4	108	0.53	0.83	33	empty
5	196	0.51	0.77	25	empty

Compared structures

4J3T · Crystal structure of barley Limit dextrinase co-crystallized with 25mM maltotetraose · 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 Q9FYY0
Elsewhere: RCSB PDB 4J3T · PDBe 4J3T · UniProt Q9FYY0

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