Research workbench
Crystal structure of the transcriptional factor from C.GLUTAMICUM at 2.2 ångström resolution
Analyse Crystal structure of the transcriptional factor from C.GLUTAMICUM at 2.2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EK5
- Type
- protein
- Length
- 457 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted transcriptional regulators
- UniProt
- Q8NLJ5
- Pockets
- 4 · best druggability 0.47
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Predicted transcriptional regulators | protein | 115 | 64% helix, 8% strand | Q8NLJ5 |
| B | Predicted transcriptional regulators | protein | 109 | 65% helix, 8% strand | Q8NLJ5 |
| C | Predicted transcriptional regulators | protein | 118 | 66% helix, 8% strand | Q8NLJ5 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.47 | 0.74 | 25 | empty |
| 2 | 65 | 0.44 | 0.81 | 14 | empty |
| 3 | 51 | 0.39 | 0.81 | 12 | empty |
| 4 | 54 | 0.27 | 0.73 | 13 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1279 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1207 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 138 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2EK5 · Crystal structure of the transcriptional factor from C.glutamicum at 2.2 angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8NLJ5
- Elsewhere: RCSB PDB 2EK5 · PDBe 2EK5 · UniProt Q8NLJ5
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