› 1b0i

X-ray diffraction
2.4Å resolution

ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS

Released:
DOI: 10.2210/pdb1b0i/pdb
PDB entry 1b0i coloured by chain, front view.
PDB entry 1b0i coloured by chain, side view.
PDB entry 1b0i coloured by chain, top view.
Source organism: Pseudoalteromonas haloplanktis
Primary publication:
Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.
Aghajari N, Feller G, Gerday C, Haser R
Structure 6 1503-16 (1998)
PMID: 9862804

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 49.38 KDa
Source organism: Pseudoalteromonas haloplanktis
Expression system: Escherichia coli
UniProt:
  • Canonical: P29957 (Residues: 25-477; Coverage: 70%)
Gene name: amy
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 56.8Å b: 80.3Å c: 120.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.217
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Life in extreme environments.
Rothschild et al. (2001)
16 more

3 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
2 more