MolNFT v1 · #40921 · protein
Crystal structure of human serine threonine kinase-10 bound to SU11274
2J7T · SERINE/THREONINE-protein kinase 10: “Crystal structure of human serine threonine kinase-10 bound to SU11274”. X-ray diffraction, 2 ligands (274, CA), 2 pockets (best druggability 0.66). MolNFT v1 #40921 on GenesisL1: 3D structure…
- PDB
- 2J7T
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase 10
- EC
- 2.7.11.1
- UniProt
- O94804
- Ligands
- 274, CA
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase 10 (EC 2.7.11.1) | protein | 285 | 44% helix, 15% strand | O94804 |
Ligands and binding sites
- 274 · (3Z)-N-(3-chlorophenyl)-3-({3,5-dimethyl-4-[(4-methylpiperazin-1-yl)carbonyl]-1H-pyrrol-2-yl}methylene)-N-methyl-2-oxoindoline-5-sulfonamide · ligand · chains A
- CA · Calcium ion · metal · 7 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 410 | 0.66 | 0.79 | 39 | CA, 274 |
| 2 | 290 | 0.54 | 0.75 | 40 | empty |
Compared structures
- 2J7T · Crystal structure of human serine threonine kinase-10 bound to SU11274 · the same entry in another collection · chain A against A, TM-score 1.00
- O94804 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase 10 (O94804) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 O94804
- Elsewhere: RCSB PDB 2J7T · PDBe 2J7T · UniProt O94804
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