Research workbench
Crystal structure of the zap-70 kinase domain in complex with staurosporine
Analyse Crystal structure of the zap-70 kinase domain in complex with staurosporine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U59
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase zap-70
- EC
- 2.7.1.112
- UniProt
- P43403
- Ligands
- STU
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase zap-70 (EC 2.7.1.112) | protein | 282 | 38% helix, 21% strand | P43403 |
Ligands and binding sites
- STU · Staurosporine · ligand · 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 | 506 | 0.66 | 0.78 | 53 | STU |
Compared structures
- 1U59 · Crystal Structure of the ZAP-70 Kinase Domain in Complex with Staurosporine · the same entry in another collection · chain A against A, TM-score 1.00
- P43403 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase zap-70 (P43403) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P43403
- Elsewhere: RCSB PDB 1U59 · PDBe 1U59 · UniProt P43403
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.