MolNFT v1 · #165519 · protein
Fak structure with AMP-pnp from single particle analysis of 2D crystals
6TY4 · Focal adhesion kinase 1: “Fak structure with AMP-pnp from single particle analysis of 2D crystals”. Electron microscopy, 2 ligands (ANP, MG), 20 pockets (best druggability 0.83). MolNFT v1 #165519 on GenesisL1: 3D structure, binding…
- PDB
- 6TY4
- Type
- protein
- Length
- 1,242 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
- Ligands
- ANP, MG
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 621 | 36% helix, 16% strand | Q00944 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 586 | 0.83 | 0.88 | 78 | empty |
| 2 | 555 | 0.82 | 0.88 | 67 | empty |
| 3 | 390 | 0.76 | 0.86 | 57 | empty |
| 4 | 341 | 0.76 | 0.87 | 54 | empty |
| 5 | 286 | 0.75 | 0.88 | 47 | empty |
Interfaces
1 interface between chains.
- A–B · 2019 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6TY4 · FAK structure with AMP-PNP from single particle analysis of 2D crystals · the same entry in another collection · chain A against A, TM-score 1.00
- Q00944 · AlphaFold monomer V2.0 prediction for focal adhesion kinase 1 (Q00944) · a predicted model of the same protein · chain A against A, TM-score 0.54
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 6TY4 · PDBe 6TY4 · UniProt Q00944
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