Research workbench
Transcriptional repressor, cour, bound to a 23-mer DNA duplex
Analyse Transcriptional repressor, cour, bound to a 23-mer DNA duplex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C2S
- Type
- protein + DNA
- Length
- 660 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator, marr family; 23-mer
- UniProt
- Q6N8V9
- Pockets
- 17 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transcriptional regulator, marr family | protein | 142 | 68% helix, 8% strand | Q6N8V9 |
| U, X | 23-mer | dna | 23 | — | — |
| V, Y | 23-mer | dna | 23 | — | — |
Pockets
17 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1046 | 0.78 | 0.80 | 77 | empty |
| 2 | 1136 | 0.76 | 0.78 | 83 | empty |
| 3 | 316 | 0.58 | 0.77 | 28 | empty |
| 4 | 70 | 0.45 | 0.82 | 20 | empty |
| 5 | 58 | 0.38 | 0.79 | 11 | empty |
Interfaces
14 interfaces between chains.
- A–D · 2599 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 2520 Ų buried · 23 hydrogen bonds · protein-protein
- X–Y · 1014 Ų buried · 99 hydrogen bonds · nucleic-nucleic
- U–V · 1012 Ų buried · 103 hydrogen bonds · nucleic-nucleic
- V–D · 478 Ų buried · 13 hydrogen bonds · protein-nucleic
Compared structures
- 6C2S · Transcriptional repressor, CouR, bound to a 23-mer DNA duplex · 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 Q6N8V9
- Elsewhere: RCSB PDB 6C2S · PDBe 6C2S · UniProt Q6N8V9
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