Research workbench
SH3-SH2 domain fragment of human BCR-abl tyrosine kinase
Analyse SH3-SH2 domain fragment of human BCR-abl tyrosine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ABL
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abl tyrosine kinase
- EC
- 2.7.1.112
- UniProt
- P00519
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abl tyrosine kinase (EC 2.7.1.112) | protein | 163 | 14% helix, 36% strand | P00519 |
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 | 292 | 0.60 | 0.78 | 37 | empty |
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 P00519
- Elsewhere: RCSB PDB 2ABL · PDBe 2ABL · UniProt P00519
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