› 6ew5

X-ray diffraction
1.95Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136047 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myelin P2 protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 133 amino acids
Theoretical weight: 14.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02689 (Residues: 1-132; Coverage: 100%)
Gene name: PMP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P212121
Unit cell:
a: 52.125Å b: 76.105Å c: 138.425Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.236
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Fatty acid-binding proteins: functional understanding and diagnostic implications.
Xu et al. (2019)
1 more

1 mention without citation

Structure and dynamics of a human myelin protein P2 portal region mutant indicate opening of the β barrel in fatty acid binding proteins.
Laulumaa et al. (2018)