› 5lxx

X-ray diffraction
1.25Å resolution

High-resolution structure of human collapsin response mediator protein 2

Released:
DOI: 10.2210/pdb5lxx/pdb
PDB entry 5lxx coloured by chain, front view.
PDB entry 5lxx coloured by chain, side view.
PDB entry 5lxx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Collapsin response mediator protein 2: high-resolution crystal structure sheds light on small-molecule binding, post-translational modifications, and conformational flexibility.
Myllykoski M, Baumann A, Hensley K, Kursula P
Amino Acids 49 747-759 (2017)
PMID: 28044206

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropyrimidinase-related protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 501 amino acids
Theoretical weight: 55.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16555 (Residues: 13-490; Coverage: 84%)
Gene names: CRMP2, DPYSL2, ULIP2
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand BTB 2 x BTB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: C2
Unit cell:
a: 141.76Å b: 97.04Å c: 92.38Å
α: 90° β: 122.54° γ: 90°
R-values:
R R work R free
0.104 0.104 0.133
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Dysregulation of CRMP2 Post-Translational Modifications Drive Its Pathological Functions.
Moutal et al. (2019)
1 more

3 mentions without citation

Tuning microtubule dynamics to enhance cancer therapy by modulating FER-mediated CRMP2 phosphorylation.
Zheng et al. (2018)
2 more