Research workbench
The kinase domain of escherichia COLI tyrosine kinase etk
Analyse The kinase domain of escherichia COLI tyrosine kinase etk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CIO
- Type
- protein
- Length
- 510 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase etk
- EC
- 2.7.10.2
- UniProt
- P38134
- Ligands
- CL
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase etk (EC 2.7.10.2) | protein | 255 | 36% helix, 16% strand | P38134 |
| D | Tyrosine-protein kinase etk (EC 2.7.10.2) | protein | 255 | 36% helix, 17% strand | P38134 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.63 | 0.94 | 17 | empty |
| 2 | 436 | 0.61 | 0.76 | 45 | empty |
| 3 | 220 | 0.54 | 0.77 | 27 | empty |
| 4 | 232 | 0.51 | 0.76 | 41 | CL |
| 5 | 222 | 0.51 | 0.76 | 32 | empty |
Interfaces
1 interface between chains.
- A–D · 879 Ų buried · 17 hydrogen bonds · protein-protein
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 P38134
- Elsewhere: RCSB PDB 3CIO · PDBe 3CIO · UniProt P38134
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