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Crystal structure of maltohexaose-producing amylase from alkalophilic bacillus SP.707.

Analyse Crystal structure of maltohexaose-producing amylase from alkalophilic bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WP6
Type
protein
Length
481 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucan 1,4-alpha-maltohexaosidase
EC
3.2.1.98
UniProt
P19571
Ligands
CA, NA, PO4
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucan 1,4-alpha-maltohexaosidase (EC 3.2.1.98)protein48127% helix, 25% strandP19571

Ligands and binding sites

  • CA · Calcium ion · metal · 3 copies · chains A
  • NA · Sodium ion · metal · chains A
  • PO4 · Phosphate ion · ion · chains A
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12230.560.7824empty

Compared structures

  • 1WP6 · Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. · the same entry in another collection · chain A against A, TM-score 1.00
  • P19571 · AlphaFold monomer V2.0 prediction for glucan 1,4-alpha- maltohexaosidase (P19571) · a predicted model of the same protein · chain A against A, TM-score 1.00

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