› 4b92

X-ray diffraction
2.9Å resolution

Crystal structure of truncated human CRMP-5 soaked with Zn

Released:
DOI: 10.2210/pdb4b92/pdb
PDB entry 4b92 coloured by chain, front view.
PDB entry 4b92 coloured by chain, side view.
PDB entry 4b92 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Insights into the oligomerization of CRMPs: crystal structure of human collapsin response mediator protein 5.
Ponnusamy R, Lohkamp B
J Neurochem 125 855-68 (2013)
PMID: 23373749

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-189652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropyrimidinase-related protein 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 484 amino acids
Theoretical weight: 52.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BPU6 (Residues: 1-483; Coverage: 86%)
Gene names: CRMP5, DPYSL5, ULIP6
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41212
Unit cell:
a: 89.5Å b: 89.5Å c: 246.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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