Research workbench
Crystal structure of the transcriptional repressor bigr from xylella fastidiosa
Analyse Crystal structure of the transcriptional repressor bigr from xylella fastidiosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PQJ
- Type
- protein
- Length
- 377 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biofilm growth-associated repressor
- UniProt
- Q9PFB1
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 3 distinct chains · 63% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Biofilm growth-associated repressor | protein | 98 | 62% helix, 12% strand | Q9PFB1 |
| B | Biofilm growth-associated repressor | protein | 91 | 64% helix, 13% strand | Q9PFB1 |
| D | Biofilm growth-associated repressor | protein | 90 | 63% helix, 13% strand | Q9PFB1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.52 | 0.74 | 37 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1769 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1767 Ų buried · 14 hydrogen bonds · protein-protein
- B–D · 123 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 105 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3PQJ · Crystal Structure of the transcriptional repressor BigR from Xylella fastidiosa · the same entry in another collection · chain D against D, TM-score 1.00
- Q9PFB1 · AlphaFold monomer V2.0 prediction for biofilm growth-associated repressor (Q9PFB1) · a predicted model of the same protein · chain C against A, TM-score 0.93
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 Q9PFB1
- Elsewhere: RCSB PDB 3PQJ · PDBe 3PQJ · UniProt Q9PFB1
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