MolNFT v1 · #171039 · protein
Focal adhesion kinase catalytic domain in complex with N-methyl-N-(2- {[2-(2-oxo-2,3-dihydro-1H-indol-5-ylamino)-5-trifluoromethyl- pyrimidin-4-ylamino]-methyl}-phenyl)-methanesulfonamide
6YR9 · Focal adhesion kinase 1: “Focal adhesion kinase catalytic domain in complex with N-methyl-N-(2…”. X-ray diffraction, 1 ligand (P9K), 10 pockets (best druggability 0.65). MolNFT v1 #171039 on GenesisL1: 3D structure, binding sites…
- PDB
- 6YR9
- Type
- protein
- Length
- 1,038 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Focal adhesion kinase 1
- EC
- 2.7.10.2
- UniProt
- Q05397
- Ligands
- P9K
- Pockets
- 10 · best druggability 0.65
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 260 | 45% helix, 17% strand | Q05397 |
| B | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 258 | 44% helix, 18% strand | Q05397 |
| C | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 258 | 45% helix, 18% strand | Q05397 |
| D | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 262 | 44% helix, 17% strand | Q05397 |
Ligands and binding sites
- P9K · N-Methyl-N-(2-{[2-(2-oxo-2,3-dihydro-1H-indol-5-ylamino)-5-trifluoromethyl-pyrimidin-4-ylamino]-methyl}-phenyl)-methanesulfonamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.65 | 0.82 | 36 | P9K |
| 2 | 281 | 0.65 | 0.81 | 40 | P9K |
| 3 | 314 | 0.64 | 0.80 | 31 | empty |
| 4 | 214 | 0.61 | 0.82 | 25 | P9K |
| 5 | 219 | 0.61 | 0.81 | 30 | P9K |
Interfaces
3 interfaces between chains.
- A–B · 683 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 605 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 566 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q05397
- Elsewhere: RCSB PDB 6YR9 · PDBe 6YR9 · UniProt Q05397
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