› 2taa

X-ray diffraction
3Å resolution

STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A

Released:
DOI: 10.2210/pdb2taa/pdb
PDB entry 2taa coloured by chain, front view.
PDB entry 2taa coloured by chain, side view.
PDB entry 2taa coloured by chain, top view.
Source organism: Aspergillus oryzae
Primary publication:
Structure and possible catalytic residues of Taka-amylase A.
Matsuura Y, Kusunoki M, Harada W, Kakudo M
J Biochem 95 697-702 (1984)
PMID: 6609921

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase A type-1/2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 478 amino acids
Theoretical weight: 52.44 KDa
Source organism: Aspergillus oryzae
Expression system: Not provided
UniProt:
  • Canonical: P0C1B3 (Residues: 22-499; Coverage: 100%)
Gene names: AO090023000944, AO090120000196, Taa-G1, Taa-G2, amy1, amy2, amyI, amyII
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 91.9Å b: 133.3Å c: 94.3Å
α: 90° β: 102.7° γ: 90°
Expression system: Not provided

Quick links

Citations

18 review citations

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
MacGregor et al. (2001)
17 more

15 mentions without citation

The Importance of Surface-Binding Site towards Starch-Adsorptivity Level in α-Amylase: A Review on Structural Point of View.
Baroroh et al. (2017)
14 more