Research workbench
C-terminal DNA binding domain of transcriptional pleiotropic repressor cody.
Analyse C-terminal DNA binding domain of transcriptional pleiotropic repressor cody. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B0L
- Type
- protein
- Length
- 287 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-sensing transcriptional pleiotropic repressor cody
- UniProt
- P39779
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-sensing transcriptional pleiotropic repressor cody | protein | 98 | 53% helix, 15% strand | P39779 |
| B | GTP-sensing transcriptional pleiotropic repressor cody | protein | 95 | 52% helix, 12% strand | P39779 |
| C | GTP-sensing transcriptional pleiotropic repressor cody | protein | 94 | 45% helix, 14% strand | P39779 |
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 | 448 | 0.70 | 0.81 | 63 | empty |
Interfaces
2 interfaces between chains.
- B–C · 385 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 123 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2B0L · C-terminal DNA binding domain of transcriptional pleiotropic repressor CodY. · the same entry in another collection · chain A against A, TM-score 1.00
- P39779 · AlphaFold monomer V2.0 prediction for GTP-sensing transcriptional pleiotropic repressor… · a predicted model of the same protein · chain C 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 P39779
- Elsewhere: RCSB PDB 2B0L · PDBe 2B0L · UniProt P39779
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