Research workbench
Crystal structure of QACR(E58Q) bound to berberine
Analyse Crystal structure of QACR(E58Q) bound to berberine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BTI
- Type
- protein
- Length
- 744 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator qacr
- UniProt
- P0A0N3
- Ligands
- BER, SO4
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, D, A, E | Hth-type transcriptional regulator qacr | protein | 186 | 63% helix, 0% strand | P0A0N3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 782 | 0.84 | 0.87 | 83 | BER |
| 2 | 746 | 0.74 | 0.79 | 69 | SO4 |
| 3 | 193 | 0.52 | 0.78 | 25 | SO4 |
| 4 | 82 | 0.44 | 0.81 | 20 | empty |
| 5 | 69 | 0.34 | 0.76 | 16 | empty |
Interfaces
3 interfaces between chains.
- B–A · 1599 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 1581 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 428 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3BTI · crystal structure of QacR(E58Q) bound to berberine · the same entry in another collection · chain B against B, TM-score 1.00
- P0A0N3 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator qacr (P0A0N3) · a predicted model of the same protein · chain B against A, TM-score 0.94
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 P0A0N3
- Elsewhere: RCSB PDB 3BTI · PDBe 3BTI · UniProt P0A0N3
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