› 6m4m

X-ray diffraction
1.7Å resolution

X-ray crystal structure of the E249Q mutan of alpha-amylase I and maltohexaose complex from Eisenia fetida

Released:
DOI: 10.2210/pdb6m4m/pdb
PDB entry 6m4m coloured by chain, front view.
PDB entry 6m4m coloured by chain, side view.
PDB entry 6m4m coloured by chain, top view.
Source organism: Eisenia fetida
Primary publication:
X-ray crystallographic structural studies of α-amylase I from Eisenia fetida.
Hirano Y, Tsukamoto K, Ariki S, Naka Y, Ueda M, Tamada T
Acta Crystallogr D Struct Biol 76 834-844 (2020)
PMID: 32876059

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103116 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 520 amino acids
Theoretical weight: 58.35 KDa
Source organism: Eisenia fetida
Expression system: Komagataella pastoris
UniProt:
  • Canonical: A0A173N065 (Residues: 18-510; Coverage: 100%)
Gene name: alpha-amylase
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
5 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand SO4 6 x SO4
Ligand PG4 1 x PG4
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P3221
Unit cell:
a: 96.809Å b: 96.809Å c: 121.233Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.158 0.18
Expression system: Komagataella pastoris

Quick links

Citations

1 citations in other articles

Novel cold-adapted raw-starch digesting α-amylases from Eisenia fetida: Gene cloning, expression, and characterization.
Tsukamoto et al. (2021)