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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.11.1)protein27339% helix, 24% strandP11309

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12110.630.8226DWC
21090.520.8222empty

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

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