MolNFT v1 · #98880 · protein
Crystal structure of PIM1 in complex with the inhibitor quercetin (resulting from displacement of SKF86002)
4LMU · SERINE/THREONINE-protein kinase pim-1: “Crystal structure of PIM1 in complex with the inhibitor quercetin (resulting from displacement of SKF86002)”. X-ray diffraction, 1 ligand (QUE), 2 pockets (best druggability 0.63). MolNFT v1…
- PDB
- 4LMU
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase pim-1
- EC
- 2.7.11.1
- UniProt
- P11309
- Ligands
- QUE
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1) | protein | 265 | 40% helix, 23% strand | P11309 |
Ligands and binding sites
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 | 204 | 0.63 | 0.83 | 28 | QUE |
| 2 | 134 | 0.52 | 0.81 | 29 | empty |
Compared structures
- 4LMU · Crystal structure of Pim1 in complex with the inhibitor Quercetin (resulting from… · 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 4LMU · PDBe 4LMU · UniProt P11309
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