Research workbench
Crystal structure of Latency Associated Peptide unbound to TGF-beta1
Analyse Crystal structure of Latency Associated Peptide unbound to TGF-beta1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P7J
- Type
- protein
- Length
- 159 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.501
- Source
- Homo sapiens
- Molecule
- Transforming growth factor beta-1 proprotein
- UniProt
- P01137
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · resolution 3.501 · 1 distinct chain · 8% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta-1 proprotein | protein | 159 | 8% helix, 43% strand | P01137 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.59 | 0.86 | 20 | empty |
Compared structures
- 6P7J · Crystal structure of latency associated peptide unbound to TGF-BETA1 · the same entry in another collection · chain A against A, TM-score 1.00
- P01137 · AlphaFold monomer V2.0 prediction for transforming growth factor beta-1 proprotein… · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P01137
- Elsewhere: RCSB PDB 6P7J · PDBe 6P7J · UniProt P01137
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.