5aej

X-ray diffraction
1.9Å resolution

Crystal structure of human Gremlin-1

Released:
Source organism: Homo sapiens
Primary publication:
Structure of Gremlin-1 and analysis of its interaction with BMP-2.
Biochem J 473 1593-604 (2016)
PMID: 27036124

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130026 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gremlin-1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 152 amino acids
Theoretical weight: 17.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O60565 (Residues: 72-184; Coverage: 71%)
Gene names: CKTSF1B1, DAND2, DRM, GREM1, PIG2
Sequence domains: DAN domain
Structure domains: Cystine-knot cytokines

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 86.816Å b: 106.135Å c: 78.521Å
α: 90° β: 121.25° γ: 90°
R-values:
R R work R free
0.181 0.179 0.208
Expression system: Escherichia coli BL21(DE3)