MolNFT v1 · #135372 · protein
Structure of TGF-BETA2 derivative with deletion of residues 52-71 and 10 single amino acid mutations (mmtgf-BETA2-7M)
5TX6 · Transforming growth factor beta-2: “Structure of TGF-BETA2 derivative with deletion of residues 52-71 and 10 single amino acid mutations…”. X-ray diffraction, 1 ligand (CA), 2 pockets (best druggability 0.43). MolNFT v1 #135372 on…
- PDB
- 5TX6
- Type
- protein
- Length
- 261 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming growth factor beta-2
- UniProt
- P27090
- Ligands
- CA
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Transforming growth factor beta-2 | protein | 92 | 10% helix, 52% strand | P27090 |
| A | Transforming growth factor beta-2 | protein | 88 | 10% helix, 55% strand | P27090 |
| C | Transforming growth factor beta-2 | protein | 81 | 11% helix, 54% strand | P27090 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.43 | 0.75 | 23 | empty |
| 2 | 108 | 0.39 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- B–A · 691 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 163 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 46 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
- 5TX6 · Structure of TGF-beta2 derivative with deletion of residues 52-71 and 10 single amino… · the same entry in another collection · chain B against B, TM-score 1.00
- P27090 · AlphaFold monomer V2.0 prediction for transforming growth factor beta-2 proprotein… · a predicted model of the same protein · chain C against A, TM-score 0.80
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 P27090
- Elsewhere: RCSB PDB 5TX6 · PDBe 5TX6 · UniProt P27090
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.