Research workbench
Crystal structure of the human PIM1 in complex with an osmium compound
Analyse Crystal structure of the human PIM1 in complex with an osmium compound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BWF
- Type
- protein
- Length
- 273 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
- 2.7.11.1
- UniProt
- P11309
- Ligands
- DWC, SO4
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1) | protein | 273 | 39% helix, 24% strand | P11309 |
Ligands and binding sites
- DWC · Pyridocarbazole cyclopentadienyl os(co) complex · ligand · chains A
- SO4 · Sulfate ion · ion · 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 | 211 | 0.63 | 0.82 | 26 | DWC |
| 2 | 109 | 0.52 | 0.82 | 22 | empty |
Compared structures
- 3BWF · Crystal structure of the human Pim1 in complex with an osmium compound · 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 3BWF · PDBe 3BWF · UniProt P11309
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