› 3vm7

X-ray diffraction
2.25Å resolution

Structure of an Alpha-Amylase from Malbranchea cinnamomea

Released:
DOI: 10.2210/pdb3vm7/pdb
PDB entry 3vm7 coloured by chain, front view.
PDB entry 3vm7 coloured by chain, side view.
PDB entry 3vm7 coloured by chain, top view.
Source organism: Malbranchea cinnamomea
Primary publication:
A novel multifunctional α-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.
Han P, Zhou P, Hu S, Yang S, Yan Q, Jiang Z
Appl Biochem Biotechnol 170 420-35 (2013)
PMID: 23536251

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125645 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 492 amino acids
Theoretical weight: 54.03 KDa
Source organism: Malbranchea cinnamomea
UniProt:
  • Canonical: K9L8F3 (Residues: 1-492; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand NAG 1 x NAG
Ligand GLC 1 x GLC
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21
Unit cell:
a: 51.9Å b: 84.94Å c: 56.41Å
α: 90° β: 105.61° γ: 90°
R-values:
R R work R free
0.147 0.143 0.191

Quick links

Citations

2 review citations

Thermophilic molds: Biology and applications.
Singh et al. (2016)
1 more

4 mentions without citation

A novel multifunctional α-amylase from the thermophilic fungus Malbranchea cinnamomea: biochemical characterization and three-dimensional structure.
Han et al. (2013)
3 more