› 1aqh

X-ray diffraction
2Å resolution

ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS

Released:
DOI: 10.2210/pdb1aqh/pdb
PDB entry 1aqh coloured by chain, front view.
PDB entry 1aqh coloured by chain, side view.
PDB entry 1aqh coloured by chain, top view.
Source organism: Pseudoalteromonas haloplanktis
Primary publication:
Crystal structures of the psychrophilic alpha-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor.
Aghajari N, Feller G, Gerday C, Haser R
Protein Sci 7 564-72 (1998)
PMID: 9541387

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 RUH2R
Spacegroup: C2221
Unit cell:
a: 71.4Å b: 138.7Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 0.204
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Some like it cold: biocatalysis at low temperatures.
Georlette et al. (2004)
10 more

12 mentions without citation

Psychrophilic enzymes: from folding to function and biotechnology.
Feller G. (2013)
11 more