› 6jl9

X-ray diffraction
2Å resolution

Crystal structure of a frog ependymin related protein

Released:
DOI: 10.2210/pdb6jl9/pdb
PDB entry 6jl9 coloured by chain, front view.
PDB entry 6jl9 coloured by chain, side view.
PDB entry 6jl9 coloured by chain, top view.
Source organism: Xenopus tropicalis
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-123651 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mammalian ependymin-related protein 1 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.84 KDa
Source organism: Xenopus tropicalis
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: F6VRB7 (Residues: 37-220; Coverage: 96%)
Gene name: epdr1
Sequence domains: Ependymin

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P6522
Unit cell:
a: 61.208Å b: 61.208Å c: 236.196Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.194 0.278
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

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

2 mentions without citation

Molecular evolution of the ependymin-related gene epdl2 in African weakly electric fish.
Losilla et al. (2023)
1 more