MolNFT v1 · #152937 · protein
Structure of the DNA binding domain of antitoxin copaso
6IYA · Transcriptional regulator copg family: “Structure of the DNA binding domain of antitoxin copaso”. X-ray diffraction, 4 pockets (best druggability 0.67). MolNFT v1 #152937 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6IYA
- Type
- protein
- Length
- 286 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator copg family
- UniProt
- Q8EGZ2
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 65% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcriptional regulator copg family | protein | 48 | 65% helix, 17% strand | Q8EGZ2 |
| C | Transcriptional regulator copg family | protein | 45 | 69% helix, 13% strand | Q8EGZ2 |
| D, E | Transcriptional regulator copg family | protein | 48 | 65% helix, 13% strand | Q8EGZ2 |
| F | Transcriptional regulator copg family | protein | 49 | 63% helix, 0% strand | Q8EGZ2 |
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 | 251 | 0.67 | 0.84 | 33 | empty |
| 2 | 287 | 0.62 | 0.80 | 35 | empty |
| 3 | 120 | 0.48 | 0.79 | 23 | empty |
| 4 | 140 | 0.40 | 0.74 | 20 | empty |
Interfaces
12 interfaces between chains.
- A–B · 1932 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1872 Ų buried · 30 hydrogen bonds · protein-protein
- B–D · 318 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 294 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 287 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6IYA · Structure of the DNA binding domain of antitoxin CopASO · 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 Q8EGZ2
- Elsewhere: RCSB PDB 6IYA · PDBe 6IYA · UniProt Q8EGZ2
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