Research workbench
Crystal structure of transcription regulatory protein slya from salmonella typhimurium in complex with salicylate ligands
Analyse Crystal structure of transcription regulatory protein slya from salmonella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DEU
- Type
- protein
- Length
- 262 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator slya
- UniProt
- P40676
- Ligands
- SAL
- Pockets
- 4 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator slya | protein | 132 | 71% helix, 7% strand | P40676 |
| B | Transcriptional regulator slya | protein | 130 | 72% helix, 5% strand | P40676 |
Ligands and binding sites
- SAL · 2-hydroxybenzoic acid · ligand · 6 copies · 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 | 289 | 0.54 | 0.74 | 22 | SAL |
| 2 | 249 | 0.53 | 0.75 | 22 | SAL |
| 3 | 146 | 0.44 | 0.75 | 21 | empty |
| 4 | 104 | 0.36 | 0.74 | 16 | SAL |
Interfaces
1 interface between chains.
- A–B · 403 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3DEU · Crystal structure of transcription regulatory protein slyA from Salmonella typhimurium in… · the same entry in another collection · chain A against A, TM-score 1.00
- P40676 · AlphaFold monomer V2.0 prediction for transcriptional regulator slya (P40676) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P40676
- Elsewhere: RCSB PDB 3DEU · PDBe 3DEU · UniProt P40676
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