› 5x1c

X-ray diffraction
2.1Å resolution

Crystal Structure of Human CRMP-2 without C-terminal Tail

Released:
DOI: 10.2210/pdb5x1c/pdb
PDB entry 5x1c coloured by chain, front view.
PDB entry 5x1c coloured by chain, side view.
PDB entry 5x1c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for CRMP2-induced axonal microtubule formation.
Niwa S, Nakamura F, Tomabechi Y, Aoki M, Shigematsu H, Matsumoto T, Yamagata A, Fukai S, Hirokawa N, Goshima Y, Shirouzu M, Nitta R
Sci Rep 7 10681 (2017)
PMID: 28878401

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: 484 amino acids
Theoretical weight: 53.05 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: P42212
Unit cell:
a: 126.687Å b: 126.687Å c: 148.219Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.202
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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