› 1hvq

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR

Released:
DOI: 10.2210/pdb1hvq/pdb
PDB entry 1hvq coloured by chain, front view.
PDB entry 1hvq coloured by chain, side view.
PDB entry 1hvq coloured by chain, top view.
Source organism: Hevea brasiliensis
Primary publication:
Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor.
Terwisscha van Scheltinga AC, Kalk KH, Beintema JJ, Dijkstra BW
Structure 2 1181-9 (1994)
PMID: 7704528

Function and Biology Details

Reactions catalysed: 
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149984 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Hevamine-A Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 29.57 KDa
Source organism: Hevea brasiliensis
UniProt:
  • Canonical: P23472 (Residues: 27-299; Coverage: 96%)
Sequence domains: Glycosyl hydrolases family 18
Structure domains: Glycosidases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 52.3Å b: 57.36Å c: 82.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.144 0.244

Quick links

Citations

10 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
9 more

4 mentions without citation

Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.
Li et al. (2010)
3 more