› 6xvs

X-ray diffraction
1.8Å 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
Molecule details ›
Chains: A, B
Length: 133 amino acids
Theoretical weight: 14.97 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

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
1 modified residue:
Ligand CSO 2 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P212121
Unit cell:
a: 55.54Å b: 65.49Å c: 82.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.167 0.225
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Disentangling glial diversity in peripheral nerves at single-nuclei resolution.
Yim et al. (2022)
3 more

1 mention without citation

Cryo-EM, X-ray diffraction, and atomistic simulations reveal determinants for the formation of a supramolecular myelin-like proteolipid lattice.
Ruskamo et al. (2020)