› 5mr4

X-ray diffraction
2.4Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126291 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neurturin Chains: A, B
Molecule details ›
Chains: A, B
Length: 102 amino acids
Theoretical weight: 11.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99748 (Residues: 96-197; Coverage: 57%)
Gene name: NRTN
Sequence domains: Transforming growth factor beta like domain
Structure domains: Cystine-knot cytokines
GDNF family receptor alpha-2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 458 amino acids
Theoretical weight: 50.93 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: O00451 (Residues: 1-458; Coverage: 99%)
Gene names: GDNFRB, GFRA2, RETL2, TRNR2
Sequence domains: GDNF/GAS1 domain

Ligands and Environments

2 bound ligands:
Ligand PEG 1 x PEG
Ligand FMT 3 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 77.81Å b: 125.811Å c: 82.722Å
α: 90° β: 101.93° γ: 90°
R-values:
R R work R free
0.196 0.195 0.22
Expression systems:
  • Escherichia coli
  • Cricetulus griseus

Quick links

Citations

4 review citations

Revisiting the Role of Neurotrophic Factors in Inflammation.
Morel et al. (2020)
3 more

5 mentions without citation

Cryo-EM analyses reveal the common mechanism and diversification in the activation of RET by different ligands.
Li et al. (2019)
4 more