Research workbench
Crystal structure analysis of focal adhesion kinase with a methanesulfonamide diaminopyrimidine inhibitor
Analyse Crystal structure analysis of focal adhesion kinase with a methanesulfonamide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BZ3
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- 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
- YAM
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Focal adhesion kinase 1 (EC 2.7.10.2) | protein | 259 | 45% helix, 17% strand | Q05397 |
Ligands and binding sites
- YAM · N-methyl-N-{3-[({2-[(2-oxo-2,3-dihydro-1H-indol-5-yl) amino]-5-(trifluoromethyl)pyrimidin-4-yl}amino) methyl]pyridin-2-yl}methanesulfonamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.61 | 0.81 | 32 | YAM |
| 2 | 116 | 0.42 | 0.76 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3BZ3 · Crystal Structure Analysis of Focal Adhesion Kinase with a Methanesulfonamide… · 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 0.96
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 3BZ3 · PDBe 3BZ3 · UniProt Q05397
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