Research workbench
AFFIMER9 co-crystalised with the ch domains of alpha actinin 2.
Analyse AFFIMER9 co-crystalised with the ch domains of alpha actinin 2. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SWT
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-actinin-2; Affimer 9
- UniProt
- P35609
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-actinin-2 | protein | 228 | 61% helix, 2% strand | P35609 |
| B | Affimer 9 | protein | 88 | 20% helix, 57% strand | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.40 | 0.76 | 19 | empty |
| 2 | 64 | 0.35 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 629 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
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 P35609
- Elsewhere: RCSB PDB 6SWT · PDBe 6SWT · UniProt P35609
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.