› 1ogo

X-ray diffraction
1.65Å resolution

Dex49A from Penicillium minioluteum complex with isomaltose

Released:
DOI: 10.2210/pdb1ogo/pdb
PDB entry 1ogo coloured by chain, front view.
PDB entry 1ogo coloured by chain, side view.
PDB entry 1ogo coloured by chain, top view.
Source organism: Talaromyces minioluteus
Primary publication:
Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex.
Larsson AM, Andersson R, Ståhlberg J, Kenne L, Jones TA
Structure 11 1111-21 (2003)
PMID: 12962629

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in dextran
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155821 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Dextranase Chain: X
Molecule details ›
Chain: X
Length: 574 amino acids
Theoretical weight: 62.44 KDa
Source organism: Talaromyces minioluteus
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P48845 (Residues: 35-608; Coverage: 98%)
Gene name: DEX
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21212
Unit cell:
a: 115.405Å b: 103.773Å c: 49.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.215
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

Recent structural insights into the expanding world of carbohydrate-active enzymes.
Davies et al. (2005)
3 more

5 mentions without citation

Causes of evolutionary rate variation among protein sites.
Echave et al. (2016)
4 more