MolNFT v1 · #82091 · protein
Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in pim-1 kinase needle screening and inhibitor design
3VBW · SERINE/THREONINE-protein kinase pim-1: “Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in pim-1 kinase needle…”. X-ray diffraction, 1 ligand (0FN), 1 pocket (best druggability 0.60). MolNFT v1…
- PDB
- 3VBW
- Type
- protein
- Length
- 264 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
- 0FN
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1) | protein | 264 | 40% helix, 22% strand | P11309 |
Ligands and binding sites
- 0FN · 1,3-dioxo-2,3-dihydro-1H-indene-2-carbonitrile · ligand · 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 | 319 | 0.60 | 0.78 | 41 | 0FN |
Compared structures
- 3VBW · Exploitation of hydrogen bonding constraints and flat hydrophobic energy landscapes in… · 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 3VBW · PDBe 3VBW · UniProt P11309
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