Research workbench
Human P56LCK tyrosine kinase complexed with phosphopeptide
Analyse Human P56LCK tyrosine kinase complexed with phosphopeptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CWE
- Type
- protein
- Length
- 208 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- P56LCK tyrosine kinase; Phosphopeptide acq-pmp-glu-glu-ile-pro
- EC
- 2.7.1.112
- UniProt
- P06239
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | P56LCK tyrosine kinase (EC 2.7.1.112) | protein | 98 | 16% helix, 31% strand | P06239 |
| B, D | Phosphopeptide acq-pmp-glu-glu-ile-pro | protein | 6 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.46 | 0.75 | 32 | empty |
Interfaces
3 interfaces between chains.
- C–D · 442 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 434 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 321 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
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 P06239
- Elsewhere: RCSB PDB 1CWE · PDBe 1CWE · UniProt P06239
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