Research workbench
Myokine structure
Analyse Myokine structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LSD
- Type
- protein
- Length
- 761 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibronectin type III domain-containing protein 5
- UniProt
- Q8NAU1
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 1% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibronectin type III domain-containing protein 5 | protein | 98 | 0% helix, 49% strand | Q8NAU1 |
| B, D, E, G, H | Fibronectin type III domain-containing protein 5 | protein | 94 | 3% helix, 52% strand | Q8NAU1 |
| C | Fibronectin type III domain-containing protein 5 | protein | 95 | 0% helix, 51% strand | Q8NAU1 |
| F | Fibronectin type III domain-containing protein 5 | protein | 98 | 0% helix, 48% strand | Q8NAU1 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 354 | 0.75 | 0.86 | 46 | empty |
| 2 | 455 | 0.65 | 0.78 | 49 | empty |
| 3 | 95 | 0.41 | 0.77 | 22 | empty |
| 4 | 100 | 0.39 | 0.76 | 20 | empty |
| 5 | 184 | 0.39 | 0.72 | 28 | empty |
Interfaces
9 interfaces between chains.
- C–D · 725 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 713 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 707 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 675 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 506 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
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 Q8NAU1
- Elsewhere: RCSB PDB 4LSD · PDBe 4LSD · UniProt Q8NAU1
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