7xb5

X-ray diffraction
3.44Å resolution

Structure of the ligand-binding domain of S. cerevisiae Upc2 in fusion with T4 lysozyme

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-133005 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin; Sterol uptake control protein 2 Chain: A
Molecule details ›
Chain: A
Length: 465 amino acids
Theoretical weight: 52.25 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12151 (Residues: 602-714, 726-897; Coverage: 31%)
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
Gene names: E, MOX4, UPC2, YD8142.14, YD8142B.05, YDR213W
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2221
Unit cell:
a: 65.744Å b: 125.085Å c: 155.272Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.258 0.301
Expression system: Escherichia coli BL21(DE3)