› 5x1d

X-ray diffraction
2.2Å resolution

Crystal Structure of T246A-N247A Human CRMP-2 Mutant

Released:
DOI: 10.2210/pdb5x1d/pdb
PDB entry 5x1d coloured by chain, front view.
PDB entry 5x1d coloured by chain, side view.
PDB entry 5x1d 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:
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 Chain: A
Molecule details ›
Chain: A
Length: 525 amino acids
Theoretical weight: 57.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16555 (Residues: 1-525; Coverage: 92%)
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 BL26B2
Spacegroup: I4122
Unit cell:
a: 114.231Å b: 114.231Å c: 193.568Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.159 0.19
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