4cns

X-ray diffraction
2.4Å resolution

Crystal structure of truncated human CRMP-4

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human CRMP-4: correction of intensities for lattice-translocation disorder.
Acta Crystallogr D Biol Crystallogr 70 1680-94 (2014)
PMID: 24914979

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
monomeric
PDBe Complex ID:
PDB-CPX-171963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropyrimidinase-related protein 3 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 480 amino acids
Theoretical weight: 52.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14195 (Residues: 13-490; Coverage: 84%)
Gene names: CRMP4, DPYSL3, DRP3, ULIP, ULIP1
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21
Unit cell:
a: 86.4Å b: 89.62Å c: 133.1Å
α: 90° β: 101.4° γ: 90°
R-values:
R R work R free
0.191 0.189 0.226
Expression system: Escherichia coli BL21(DE3)