› 6jld

X-ray diffraction
2Å resolution

Crystal structure of a human ependymin related protein

Released:
DOI: 10.2210/pdb6jld/pdb
PDB entry 6jld coloured by chain, front view.
PDB entry 6jld coloured by chain, side view.
PDB entry 6jld coloured by chain, top view.
Source organism: Homo sapiens
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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193955 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mammalian ependymin-related protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 198 amino acids
Theoretical weight: 23.14 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9UM22 (Residues: 38-224; Coverage: 100%)
Gene names: EPDR1, MERP1, UCC1
Sequence domains: Ependymin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P43
Unit cell:
a: 55.858Å b: 55.858Å c: 273.769Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.235
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)