Research workbench
The structure of the FOLLISTATIN:ACTIVIN complex
Analyse The structure of the FOLLISTATIN:ACTIVIN complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B0U
- Type
- protein
- Length
- 799 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibin beta a chain; Follistatin
- UniProt
- P08476, P19883
- Ligands
- IR3
- Pockets
- 19 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 17% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Inhibin beta a chain | protein | 116 | 16% helix, 41% strand | P08476 |
| C | Follistatin | protein | 287 | 17% helix, 25% strand | P19883 |
| D | Follistatin | protein | 280 | 17% helix, 24% strand | P19883 |
Ligands and binding sites
- IR3 · Iridium (III) ion · metal · 5 copies · chains A, B, C
- MLI · Malonate ion · additive · 4 copies · chains A, D
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 510 | 0.69 | 0.79 | 40 | empty |
| 2 | 492 | 0.65 | 0.77 | 42 | empty |
| 3 | 261 | 0.61 | 0.80 | 49 | empty |
| 4 | 157 | 0.59 | 0.83 | 20 | MLI |
| 5 | 148 | 0.57 | 0.82 | 20 | MPD |
Interfaces
6 interfaces between chains.
- A–B · 1561 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 1453 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1328 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 731 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 328 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 45 disulfide (disulfide).
Compared structures
- 2B0U · The Structure of the Follistatin:Activin Complex · the same entry in another collection · chain A against A, TM-score 1.00
- P19883 · AlphaFold monomer V2.0 prediction for follistatin (P19883) · a predicted model of the same protein · chain C against A, TM-score 0.96
- 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 0.74
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 P19883
- Elsewhere: RCSB PDB 2B0U · PDBe 2B0U · UniProt P08476 · UniProt P19883
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