5w0p

X-ray diffraction
3.01Å resolution

Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-132952 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Endolysin; Rhodopsin; S-arrestin Chains: A, B
Molecule details ›
Chains: A, B
Length: 906 amino acids
Theoretical weight: 101.02 KDa
Source organisms: Expression system: Homo sapiens
UniProt:
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
  • Canonical: P08100 (Residues: 1-348; Coverage: 100%)
  • Canonical: P20443 (Residues: 10-392; Coverage: 95%)
Gene names: E, OPN2, RHO, Sag
Sequence domains:
Endolysin; Rhodopsin; S-arrestin Chains: C, D
Molecule details ›
Chains: C, D
Length: 906 amino acids
Theoretical weight: 100.94 KDa
Source organisms: Expression system: Homo sapiens
UniProt:
  • Canonical: P00720 (Residues: 2-161; Coverage: 98%)
  • Canonical: P08100 (Residues: 1-348; Coverage: 100%)
  • Canonical: P20443 (Residues: 10-392; Coverage: 95%)
Gene names: E, OPN2, RHO, Sag
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLAC LCLS BEAMLINE CXI
Spacegroup: P212121
Unit cell:
a: 109.24Å b: 109.24Å c: 452.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.234 0.272
Expression system: Homo sapiens