› 6jla

X-ray diffraction
2.4Å resolution

Crystal structure of a mouse ependymin related protein

Released:
DOI: 10.2210/pdb6jla/pdb
PDB entry 6jla coloured by chain, front view.
PDB entry 6jla coloured by chain, side view.
PDB entry 6jla coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder.
Park JK, Kim KY, Sim YW, Kim YI, Kim JK, Lee C, Han J, Kim CU, Lee JE, Park S
IUCrJ 6 729-739 (2019)
PMID: 31316816

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Mammalian ependymin-related protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 198 amino acids
Theoretical weight: 22.95 KDa
Source organism: Mus musculus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q99M71 (Residues: 38-224; Coverage: 100%)
Gene names: Epdr1, Epdr2, Merp1, Merp2
Sequence domains: Ependymin

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
1 bound ligand:
Ligand NAG 4 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21
Unit cell:
a: 56.966Å b: 59.671Å c: 137.336Å
α: 90° β: 101.29° γ: 90°
R-values:
R R work R free
0.188 0.185 0.24
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

New players of the adipose secretome: Therapeutic opportunities and challenges.
Coassolo et al. (2022)
3 other articles

1 mention without citation

Structures of three ependymin-related proteins suggest their function as a hydrophobic molecule binder.
Park et al. (2019)