PDBe 3my0

X-ray diffraction
2.65Å resolution

Crystal structure of the ACVRL1 (ALK1) kinase domain bound to LDN-193189

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein kinase receptor R3 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 305 amino acids
Theoretical weight: 34.81 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P37023 (Residues: 195-497; Coverage: 63%)
Gene names: ACVRL1, ACVRLK1, ALK1
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P32
Unit cell:
a: 118.77Å b: 118.77Å c: 510.791Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.207 0.247
Expression system: Spodoptera frugiperda