MolNFT v1 · #19609 · protein
Structural analysis of the lymphocyte-specific kinase lck in complex with non-selective and src family selective kinase inhibitors
1QPC · Tyrosine-protein kinase lck: “Structural analysis of the lymphocyte-specific kinase lck in complex with non-selective and src family…”. X-ray diffraction, 2 ligands (ANP, SO4), 1 pocket (best druggability 0.61). MolNFT v1 #19609 on…
- PDB
- 1QPC
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase lck
- EC
- 2.7.10.2
- UniProt
- P06239
- Ligands
- ANP, SO4
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase lck (EC 2.7.10.2) | protein | 271 | 39% helix, 20% strand | P06239 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 351 | 0.61 | 0.78 | 37 | ANP, EDO |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 1QPC · Structural analysis of the lymphocyte-specific kinase lck in complex with non-selective… · the same entry in another collection · chain A against A, TM-score 1.00
- P06239 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase lck (P06239) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P06239
- Elsewhere: RCSB PDB 1QPC · PDBe 1QPC · UniProt P06239
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