Research workbench
A darpin semi-rigidly fused to the 3TEL crystallization chaperone
Analyse A darpin semi-rigidly fused to the 3TEL crystallization chaperone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N2B
- Type
- protein
- Length
- 806 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription factor ETV6,TRANSCRIPTION factor ETV6, transcription factor…
- UniProt
- P41212
- Pockets
- 3 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription factor ETV6,TRANSCRIPTION factor ETV6, transcription factor ETV6,3TEL-rigid-darpin | protein | 402 | 61% helix, 0% strand | P41212 |
| B | Transcription factor ETV6,TRANSCRIPTION factor ETV6, transcription factor ETV6,3TEL-rigid-darpin | protein | 404 | 60% helix, 0% strand | P41212 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.44 | 0.81 | 14 | empty |
| 2 | 89 | 0.35 | 0.74 | 13 | empty |
| 3 | 52 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 609 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 7N2B · A DARPin semi-rigidly fused to the 3TEL crystallization chaperone · the same entry in another collection · chain A against A, TM-score 1.00
- P41212 · AlphaFold monomer V2.0 prediction for transcription factor ETV6 (P41212) · a predicted model of the same protein · chain A against A, TM-score 0.28
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 P41212
- Elsewhere: RCSB PDB 7N2B · PDBe 7N2B · UniProt P41212
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