Research workbench
The crystal structure of the BET3-TRS33-BET5-TRS23 complex.
Analyse The crystal structure of the BET3-TRS33-BET5-TRS23 complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J3T
- Type
- protein
- Length
- 661 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trafficking protein particle complex subunit 3; Trafficking protein particle complex…
- UniProt
- O55013, O75865, Q5NCF2, Q9Y296
- Ligands
- PLM
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trafficking protein particle complex subunit 3 | protein | 158 | 48% helix, 18% strand | O55013 |
| B | Trafficking protein particle complex subunit 6A | protein | 152 | 45% helix, 18% strand | O75865 |
| C | Trafficking protein particle complex subunit 1 | protein | 141 | 35% helix, 21% strand | Q5NCF2 |
| D | Trafficking protein particle complex subunit 4 | protein | 210 | 27% helix, 28% strand | Q9Y296 |
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
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.83 | 0.96 | 30 | PLM |
| 2 | 849 | 0.77 | 0.80 | 77 | empty |
| 3 | 126 | 0.48 | 0.79 | 35 | empty |
| 4 | 219 | 0.48 | 0.74 | 31 | empty |
| 5 | 124 | 0.47 | 0.78 | 26 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1894 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1220 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 808 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 538 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 417 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 lipid (palmitoylation).
Compared structures
- 2J3T · The crystal structure of the bet3-trs33-bet5-trs23 complex. · the same entry in another collection · chain D against D, TM-score 1.00
- Q5NCF2 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 1… · a predicted model of the same protein · chain C against A, TM-score 0.99
- 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 0.96
- Q9Y296 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 4… · a predicted model of the same protein · chain D against A, TM-score 0.92
- 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 0.89
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 O75865
- Every structure of UniProt Q5NCF2
- Every structure of UniProt Q9Y296
- Elsewhere: RCSB PDB 2J3T · PDBe 2J3T · UniProt O55013 · UniProt O75865 · UniProt Q5NCF2 · UniProt Q9Y296
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