› 2amg

X-ray diffraction
2Å resolution

STRUCTURE OF HYDROLASE (GLYCOSIDASE)

Released:
DOI: 10.2210/pdb2amg/pdb
PDB entry 2amg coloured by chain, front view.
PDB entry 2amg coloured by chain, side view.
PDB entry 2amg coloured by chain, top view.
Source organism: Pseudomonas stutzeri
Primary publication:
Crystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Morishita Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M, Sakai S
J Mol Biol 267 661-72 (1997)
PMID: 9126844

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends
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-146628 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucan 1,4-alpha-maltotetraohydrolase Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 46.58 KDa
Source organism: Pseudomonas stutzeri
UniProt:
  • Canonical: P13507 (Residues: 22-439; Coverage: 79%)
Gene name: amyP
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 65.6Å b: 170.5Å c: 46.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available

Quick links

Citations

4 review citations

Fold change in evolution of protein structures.
Grishin NV. (2001)
3 more

2 mentions without citation

Active site detection by spatial conformity and electrostatic analysis--unravelling a proteolytic function in shrimp alkaline phosphatase.
Chakraborty et al. (2011)
1 more