› 4iap

X-ray diffraction
2.3Å resolution

Crystal structure of PH domain of Osh3 from Saccharomyces cerevisiae

Released:
DOI: 10.2210/pdb4iap/pdb
PDB entry 4iap coloured by chain, front view.
PDB entry 4iap coloured by chain, side view.
PDB entry 4iap coloured by chain, top view.
Source organisms:
Primary publication:
Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins.
Tong J, Yang H, Yang H, Eom SH, Im YJ
Structure 21 1203-13 (2013)
PMID: 23791945

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:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-132984 (preferred)
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: P00720 (Residues: 2-161; Coverage: 98%)
  • Canonical: P38713 (Residues: 237-315; Coverage: 8%)
Gene names: E, OSH3, YHR073W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
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)

Quick links

Citations

25 review citations

Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.
Wong et al. (2019)
24 more

2 mentions without citation

ORP5 and ORP8 bind phosphatidylinositol-4, 5-biphosphate (PtdIns(4,5)P 2) and regulate its level at the plasma membrane.
Ghai et al. (2017)
1 more