Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (activin receptor type II) (EC 2.7.1.-) | protein | 92 | 8% helix, 45% strand | P27038 |
| B | Protein (activin receptor type II) (EC 2.7.1.-) | protein | 94 | 7% helix, 44% strand | P27038 |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P27038
- Elsewhere: RCSB PDB 1BTE · PDBe 1BTE · UniProt P27038
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