› 5fwv

X-ray diffraction
3.2Å resolution

Wnt modulator Kremen crystal form III at 3.2A

Released:
DOI: 10.2210/pdb5fwv/pdb
PDB entry 5fwv coloured by chain, front view.
PDB entry 5fwv coloured by chain, side view.
PDB entry 5fwv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight into Ternary Complex Formation with LRP6 and Dickkopf.
Zebisch M, Jackson VA, Zhao Y, Jones EY
Structure 24 1599-605 (2016)
PMID: 27524201

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kremen protein 1 Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 44.55 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: Q96MU8 (Residues: 29-324, 326-373; Coverage: 76%)
Gene names: KREMEN, KREMEN1, KRM1
Sequence domains:
Structure domains: Plasminogen Kringle 4

Ligands and Environments

2 bound ligands:
Ligand CL 5 x CL
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P41212
Unit cell:
a: 67.844Å b: 67.844Å c: 198.193Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.195 0.265
Expression system: Homo sapiens

Quick links

Citations

5 review citations

Rationale for targeting the Wnt signalling modulator Dickkopf-1 for oncology.
Kagey et al. (2017)
4 more

3 mentions without citation

Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIV = O formation in bacterial dye-decolorizing peroxidases.
Lučić et al. (2021)
2 more