Research workbench
Crystal structure of the apo form transcription factor
Analyse Crystal structure of the apo form transcription factor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IPX
- Type
- protein
- Length
- 778 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aimr transcriptional regulator
- UniProt
- O64094
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aimr transcriptional regulator | protein | 390 | 71% helix, 0% strand | O64094 |
| B | Aimr transcriptional regulator | protein | 388 | 72% helix, 0% strand | O64094 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 798 | 0.78 | 0.81 | 45 | empty |
| 2 | 776 | 0.77 | 0.81 | 45 | empty |
| 3 | 732 | 0.71 | 0.77 | 70 | empty |
| 4 | 148 | 0.46 | 0.77 | 20 | empty |
| 5 | 162 | 0.40 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 368 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6IPX · Crystal structure of the apo form transcription factor · 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 O64094
- Elsewhere: RCSB PDB 6IPX · PDBe 6IPX · UniProt O64094
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