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:
Source organism: Aspergillus oryzae
Entry authors: Vujicic-Zagar A, Dijkstra BW

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:

Structure analysis Details

Assembly composition:
monomeric (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 : NEW Components: GLC
2 bound ligands:
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