MolNFT v1 · #58471 · protein
X-ray structure of activin in complex with FSTL3
3B4V · Inhibin beta a chain: “X-ray structure of activin in complex with FSTL3”. X-ray diffraction, 2 ligands (NAG, SO4), 20 pockets (best druggability 0.81). MolNFT v1 #58471 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3B4V
- Type
- protein
- Length
- 1,280 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibin beta a chain; Follistatin-like 3
- UniProt
- P08476, O95633
- Ligands
- NAG, SO4
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 7 distinct chains · 15% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibin beta a chain | protein | 109 | 15% helix, 43% strand | P08476 |
| B | Inhibin beta a chain | protein | 114 | 15% helix, 42% strand | P08476 |
| C, G | Follistatin-like 3 | protein | 206 | 15% helix, 27% strand | O95633 |
| D | Follistatin-like 3 | protein | 213 | 15% helix, 27% strand | O95633 |
| E | Inhibin beta a chain | protein | 107 | 14% helix, 44% strand | P08476 |
| F | Inhibin beta a chain | protein | 114 | 16% helix, 42% strand | P08476 |
| H | Follistatin-like 3 | protein | 211 | 15% helix, 27% strand | O95633 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains C, D, G
- SO4 · Sulfate ion · ion · chains C
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, C, D, B, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.81 | 0.89 | 65 | empty |
| 2 | 715 | 0.79 | 0.84 | 90 | empty |
| 3 | 480 | 0.75 | 0.84 | 64 | empty |
| 4 | 489 | 0.67 | 0.78 | 72 | empty |
| 5 | 411 | 0.67 | 0.80 | 51 | empty |
Interfaces
16 interfaces between chains.
- E–F · 1474 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1465 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1337 Ų buried · 19 hydrogen bonds · protein-protein
- F–G · 1326 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 1233 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 70 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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 O95633
- Elsewhere: RCSB PDB 3B4V · PDBe 3B4V · UniProt P08476 · UniProt O95633
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