Research workbench
The crystal structure of the BET3-TRS31 heterodimer.
Analyse The crystal structure of the BET3-TRS31 heterodimer. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J3R
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trafficking protein particle complex subunit 3; Zgc 92866
- UniProt
- O55013, Q6DGL5
- Ligands
- PLM, NO3
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex subunit 3 | protein | 158 | 46% helix, 18% strand | O55013 |
| B | Zgc 92866 | protein | 157 | 52% helix, 17% strand | Q6DGL5 |
Ligands and binding sites
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 | 209 | 0.81 | 0.94 | 32 | PLM |
| 2 | 221 | 0.51 | 0.76 | 32 | NO3 |
| 3 | 150 | 0.46 | 0.76 | 18 | empty |
| 4 | 60 | 0.33 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1631 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (palmitoylation).
Compared structures
- 2J3R · The crystal structure of the bet3-trs31 heterodimer. · the same entry in another collection · chain A against A, TM-score 1.00
- O55013 · 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 0.95
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 O55013
- Every structure of UniProt Q6DGL5
- Elsewhere: RCSB PDB 2J3R · PDBe 2J3R · UniProt O55013 · UniProt Q6DGL5
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