PDBe 4iap

X-ray diffraction
2.3Å resolution

Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae

Released:

Function and Biology Details

Reaction catalysed:
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:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Oxysterol-binding protein homolog 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 29.75 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P38713 (Residues: 237-315; Coverage: 8%)
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
Gene names: E, OSH3, YHR073W
Sequence domains: Phage lysozyme
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 98.033Å b: 91.307Å c: 84.13Å
α: 90° β: 81.42° γ: 90°
R-values:
R R work R free
0.242 0.242 0.274
Expression system: Escherichia coli BL21(DE3)