Research workbench
Crystal structure of kinase PIM1 with P123M mutation
Analyse Crystal structure of kinase PIM1 with P123M mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YXS
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene SERINE/THREONINE-protein kinase pim-1
- EC
- 2.7.1.37
- UniProt
- P11309
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.1.37) | protein | 274 | 37% helix, 23% strand | P11309 |
Ligands and binding sites
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.65 | 0.83 | 25 | empty |
| 2 | 99 | 0.47 | 0.81 | 23 | empty |
| 3 | 65 | 0.44 | 0.81 | 13 | empty |
Compared structures
- 1YXS · Crystal Structure of Kinase Pim1 with P123M mutation · the same entry in another collection · chain A against A, TM-score 1.00
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 P11309
- Elsewhere: RCSB PDB 1YXS · PDBe 1YXS · UniProt P11309
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