GL1X · GenesisL1 explorer

Research workbench

Crystal structure of maltogenic amylase from S.MARINUS

Analyse Crystal structure of maltogenic amylase from S.MARINUS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4AEE
Type
protein
Length
1,368 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha amylase, catalytic region
EC
3.2.1.133
UniProt
A3DM60
Pockets
13 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAlpha amylase, catalytic region (EC 3.2.1.133)protein68427% helix, 30% strandA3DM60

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111610.760.7981empty
28360.760.8079empty
37200.750.8066empty
45460.690.7843empty
55400.690.7950empty

Interfaces

1 interface between chains.

  • A–B · 792 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 4AEE · Crystal structure of maltogenic amylase from S.MARINUS · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.