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Crystal structure of the extracellular domain of the type II activin receptor

Analyse Crystal structure of the extracellular domain of the type II activin receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BTE
Type
protein
Length
186 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (activin receptor type II)
EC
2.7.1.-
UniProt
P27038
Ligands
NAG

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (activin receptor type II) (EC 2.7.1.-)protein928% helix, 45% strandP27038
BProtein (activin receptor type II) (EC 2.7.1.-)protein947% helix, 44% strandP27038

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 10 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 1BTE · Crystal structure of the extracellular domain of the type II activin receptor · the same entry in another collection · chain A against A, TM-score 1.00
  • P27038 · AlphaFold monomer V2.0 prediction for activin receptor type-2A (P27038) · a predicted model of the same protein · chain B against A, TM-score 0.90

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