› 2gvy

X-ray diffraction
1.8Å resolution

Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution

Released:
DOI: 10.2210/pdb2gvy/pdb
PDB entry 2gvy coloured by chain, front view.
PDB entry 2gvy coloured by chain, side view.
PDB entry 2gvy coloured by chain, top view.
Source organism: Aspergillus oryzae
Primary publication:
Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution.
Vujicić-Zagar A, Dijkstra BW
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 716-21 (2006)
PMID: 16880540

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
Macromolecules (3 distinct):
Alpha-amylase A type-1/2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 478 amino acids
Theoretical weight: 52.53 KDa
Source organism: Aspergillus oryzae
Expression system: Aspergillus oryzae
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

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 65.451Å b: 101.149Å c: 75.185Å
α: 90° β: 103.89° γ: 90°
R-values:
R R work R free
0.165 0.162 0.21
Expression system: Aspergillus oryzae

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Citations

1 review citation

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
10 other articles

9 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)
8 more