1cpm

X-ray diffraction
2Å resolution

NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucanase Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.88 KDa
Source organism: Paenibacillus macerans
Expression system: Not provided
UniProt:
  • Canonical: P23904 (Residues: 82-237; Coverage: 73%)
Structure domains: Jelly Rolls

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 39.43Å b: 44.3Å c: 128.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.153 not available
Expression system: Not provided