Research workbench
Crystal structure of the bet3-trs33 heterodimer
Analyse Crystal structure of the bet3-trs33 heterodimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C0J
- Type
- protein
- Length
- 303 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- HOMO SAPIENS
- Molecule
- Trafficking protein particle complex subunit 3; R32611_2
- UniProt
- O43617, O75865
- Ligands
- PLM
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex subunit 3 | protein | 161 | 47% helix, 17% strand | O43617 |
| B | R32611_2 | protein | 142 | 55% helix, 15% strand | O75865 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.82 | 0.95 | 30 | PLM |
| 2 | 200 | 0.52 | 0.77 | 26 | empty |
| 3 | 54 | 0.29 | 0.75 | 11 | empty |
| 4 | 51 | 0.27 | 0.73 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1289 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (palmitoylation).
Compared structures
- 2C0J · Crystal structure of the BET3-TRS33 heterodimer · the same entry in another collection · chain A against A, TM-score 1.00
- O75865 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 6A… · a predicted model of the same protein · chain B against A, TM-score 0.96
- O43617 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 3… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O43617
- Every structure of UniProt O75865
- Elsewhere: RCSB PDB 2C0J · PDBe 2C0J · UniProt O43617 · UniProt O75865
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