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Crystal structure of isomaltase from saccharomyces cerevisiae

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

PDB: 3AJ7
Type: protein
Length: 586 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oligo-1,6-glucosidase
EC: 3.2.1.10
UniProt: P53051
Ligands: CA
Pockets: 6 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oligo-1,6-glucosidase (EC 3.2.1.10)	protein	586	33% helix, 19% strand	P53051

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	400	0.78	0.87	46	empty
2	193	0.57	0.81	27	empty
3	105	0.57	0.85	19	empty
4	115	0.36	0.73	19	empty
5	79	0.35	0.75	11	empty

Compared structures

3AJ7 · Crystal Structure of isomaltase from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P53051 · AlphaFold monomer V2.0 prediction for oligo-1,6-glucosidase IMA1 (P53051) · 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 P53051
Elsewhere: RCSB PDB 3AJ7 · PDBe 3AJ7 · UniProt P53051

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