Research workbench
Crystal structure of the focal adhesion targeting domain of focal adhesion kinase
Analyse Crystal structure of the focal adhesion targeting domain of focal adhesion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K05
- Type
- protein
- Length
- 419 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Focal adhesion kinase 1
- EC
- 2.7.1.112
- UniProt
- Q05397
- Pockets
- 6 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Focal adhesion kinase 1 (EC 2.7.1.112) | protein | 135 | 82% helix, 0% strand | Q05397 |
| B | Focal adhesion kinase 1 (EC 2.7.1.112) | protein | 142 | 81% helix, 0% strand | Q05397 |
| C | Focal adhesion kinase 1 (EC 2.7.1.112) | protein | 142 | 80% helix, 0% strand | Q05397 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.49 | 0.75 | 29 | empty |
| 2 | 98 | 0.41 | 0.77 | 14 | empty |
| 3 | 75 | 0.40 | 0.79 | 17 | empty |
| 4 | 74 | 0.40 | 0.79 | 17 | empty |
| 5 | 101 | 0.39 | 0.76 | 15 | empty |
Interfaces
2 interfaces between chains.
- A–B · 676 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 659 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1K05 · Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase · the same entry in another collection · chain A against A, TM-score 1.00
- Q05397 · AlphaFold monomer V2.0 prediction for focal adhesion kinase 1 (Q05397) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q05397
- Elsewhere: RCSB PDB 1K05 · PDBe 1K05 · UniProt Q05397
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