› 5m0w

X-ray diffraction
1.39Å resolution

N-terminal domain of mouse Shisa 3

Released:
DOI: 10.2210/pdb5m0w/pdb
PDB entry 5m0w coloured by chain, front view.
PDB entry 5m0w coloured by chain, side view.
PDB entry 5m0w coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Ab initio solution of macromolecular crystal structures without direct methods.
McCoy AJ, Oeffner RD, Wrobel AG, Ojala JR, Tryggvason K, Lohkamp B, Read RJ
Proc Natl Acad Sci U S A 114 3637-3641 (2017)
PMID: 28325875

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein shisa-3 homolog Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.04 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q3UPR0 (Residues: 22-95; Coverage: 34%)
Gene name: Shisa3
Sequence domains: Wnt and FGF inhibitory regulator

Ligands and Environments

5 bound ligands:
Ligand SO4 2 x SO4
Ligand GOL 3 x GOL
Ligand EDO 3 x EDO
Ligand MES 1 x MES
Ligand PEG 1 x PEG
1 modified residue:
Ligand PCA 1 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P43212
Unit cell:
a: 59.765Å b: 59.765Å c: 48.591Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.115 0.137
Expression system: Trichoplusia ni

Quick links

Citations

1 review citation

Implications of AlphaFold2 for crystallographic phasing by molecular replacement.
McCoy et al. (2022)
23 other articles

2 mentions without citation

On the application of the expected log-likelihood gain to decision making in molecular replacement.
Oeffner et al. (2018)
1 more