MolNFT v1 · #32181 · protein

Human PIM1 phosphorylated on SER261

2BIK · Proto-oncogene SERINE/THREONINE-protein kinase pim-1: “Human PIM1 phosphorylated on SER261”. X-ray diffraction, 2 ligands (BI1, CL), 3 pockets (best druggability 0.68). MolNFT v1 #32181 on GenesisL1: 3D structure, binding sites and…

PDB: 2BIK
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: 2.7.1.37
UniProt: P11309
Ligands: BI1, CL
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Proto-oncogene SERINE/THREONINE-protein kinase pim-1 (EC 2.7.1.37)	protein	273	40% helix, 23% strand	P11309

Ligands and binding sites

BI1 · 3-{1-[3-(dimethylamino)propyl]-1H-indol-3-yl}-4-(1H-indol-3-yl)-1H-pyrrole-2,5-dione · ligand · chains B
CL · Chloride ion · ion · 2 copies · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	363	0.68	0.81	48	BI1, CL
2	57	0.29	0.75	11	empty
3	51	0.27	0.75	15	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

2BIK · Human Pim1 phosphorylated on Ser261 · the same entry in another collection · chain B against B, 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 2BIK · PDBe 2BIK · UniProt P11309

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