PDBe 4cnu

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF WT HUMAN CRMP-4 from lattice translocation

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

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydropyrimidinase-related protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 570 amino acids
Theoretical weight: 62.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14195 (Residues: 1-570; Coverage: 100%)
Gene names: CRMP4, DPYSL3, DRP3, ULIP, ULIP1
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: MAX II BEAMLINE I911-3
Spacegroup: P21212
Unit cell:
a: 96.24Å b: 108.22Å c: 118.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.255 0.295
Expression system: Escherichia coli BL21(DE3)