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Crystal structure of a transcriptional regulator
Analyse Crystal structure of a transcriptional regulator in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VI0
- Type
- protein
- Length
- 377 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator
- UniProt
- P94548
- Ligands
- DCC
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator | protein | 189 | 78% helix, 1% strand | P94548 |
| B | Transcriptional regulator | protein | 188 | 77% helix, 1% strand | P94548 |
Ligands and binding sites
- DCC · Dodecyl-coa · ligand · 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 | 386 | 0.80 | 0.89 | 48 | DCC |
| 2 | 142 | 0.55 | 0.82 | 28 | empty |
| 3 | 98 | 0.45 | 0.79 | 17 | empty |
| 4 | 58 | 0.27 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2119 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
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 P94548
- Elsewhere: RCSB PDB 1VI0 · PDBe 1VI0 · UniProt P94548
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