Research workbench
Fak structure from single particle analysis of 2D crystals
Analyse Fak structure from single particle analysis of 2D crystals in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TY3
- Type
- protein
- Length
- 1,200 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Focal adhesion kinase 1
- EC
- 2.7.10.2
- UniProt
- Q00944
- Pockets
- 18 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 600 | 38% helix, 16% strand | Q00944 |
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1151 | 0.86 | 0.86 | 125 | empty |
| 2 | 1043 | 0.83 | 0.84 | 129 | empty |
| 3 | 943 | 0.82 | 0.84 | 82 | empty |
| 4 | 56 | 0.67 | 0.95 | 19 | empty |
| 5 | 148 | 0.66 | 0.87 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1724 Ų buried · 4 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 Q00944
- Elsewhere: RCSB PDB 6TY3 · PDBe 6TY3 · UniProt Q00944
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.