Research workbench
Structure of activin a in complex with an actriib-ALK4 fusion reveal insight into activin receptor interactions
Analyse Structure of activin a in complex with an actriib-ALK4 fusion reveal insight… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OLY
- Type
- protein
- Length
- 729 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibin beta a chain; Activin receptor type-2B; Fab heavy chain; Activin receptor…
- EC
- 2.7.11.30
- UniProt
- P08476, Q13705, P36896
- Ligands
- NAG, MAN
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 5 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibin beta a chain | protein | 116 | 16% helix, 43% strand | P08476 |
| C | Activin receptor type-2B (EC 2.7.11.30) | protein | 95 | 6% helix, 43% strand | Q13705 |
| H | Fab heavy chain | protein | 219 | 5% helix, 51% strand | — |
| K | Activin receptor type-1B (EC 2.7.11.30) | protein | 79 | 8% helix, 34% strand | P36896 |
| L | Fab light chain | protein | 220 | 6% helix, 49% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains C, H
- MAN · alpha-D-mannopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 631 | 0.63 | 0.74 | 63 | empty |
| 2 | 201 | 0.52 | 0.77 | 33 | empty |
| 3 | 196 | 0.51 | 0.77 | 28 | empty |
| 4 | 56 | 0.30 | 0.76 | 13 | empty |
| 5 | 65 | 0.27 | 0.72 | 17 | empty |
Interfaces
5 interfaces between chains.
- H–L · 1836 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 746 Ų buried · 2 hydrogen bonds · protein-protein
- C–H · 658 Ų buried · 13 hydrogen bonds · protein-protein
- A–K · 400 Ų buried · 1 hydrogen bond · protein-protein
- C–L · 183 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 7OLY · Structure of activin A in complex with an ActRIIB-Alk4 fusion reveal insight into activin… · the same entry in another collection · chain L against L, TM-score 1.00
- Q13705 · AlphaFold monomer V2.0 prediction for activin receptor type-2B (Q13705) · a predicted model of the same protein · chain C against A, TM-score 0.94
- P36896 · AlphaFold monomer V2.0 prediction for activin receptor type-1B (P36896) · a predicted model of the same protein · chain K against A, TM-score 0.89
- P08476 · AlphaFold monomer V2.0 prediction for inhibin beta a chain (P08476) · a predicted model of the same protein · chain A against A, TM-score 0.75
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 P08476
- Every structure of UniProt Q13705
- Every structure of UniProt P36896
- Elsewhere: RCSB PDB 7OLY · PDBe 7OLY · UniProt P08476 · UniProt Q13705 · UniProt P36896
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