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Crystal structure of anoxybacillus alpha-amylase provides insights into a new glycosyl hydrolase subclass

Analyse Crystal structure of anoxybacillus alpha-amylase provides insights into a new… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5A2B
Type: protein
Length: 452 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Anoxybacillus alpha-amylase
EC: 3.2.1.1
UniProt: I1VWH9
Ligands: GLC, CA
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Anoxybacillus alpha-amylase (EC 3.2.1.1)	protein	452	36% helix, 22% strand	I1VWH9

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
CA · Calcium ion · metal · 4 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	244	0.59	0.79	24	GLC

Compared structures

5A2B · Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl… · 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 I1VWH9
Elsewhere: RCSB PDB 5A2B · PDBe 5A2B · UniProt I1VWH9

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