Research workbench
Pim-1 kinase in complex with a selective N-substituted 7-azaindole inhibitor
Analyse Pim-1 kinase in complex with a selective N-substituted 7-azaindole inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KCX
- Type
- protein
- Length
- 272 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
- 6S3
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1) | protein | 272 | 38% helix, 24% strand | P11309 |
Ligands and binding sites
- 6S3 · 4-chloranyl-1-methyl-2-[4-(4-methylpiperazin-1-yl) phenyl]pyrrolo[2,3-b]pyridine-6-carboxamide · ligand · chains A
- IMD · Imidazole · additive · chains A
- ACT · Acetate ion · additive · 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 | 335 | 0.67 | 0.81 | 50 | 6S3 |
Compared structures
- 5KCX · Pim-1 kinase in Complex with a Selective N-substituted 7-azaindole Inhibitor · 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 5KCX · PDBe 5KCX · UniProt P11309
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