MolNFT v1 · #32745 · protein

Crystal structure of the human PIM1 in complex with a ruthenium organometallic ligand RU1

2BZH · Proto-oncogene serine threonine protein kinase PIM1: “Crystal structure of the human PIM1 in complex with a ruthenium organometallic ligand RU1”. X-ray diffraction, 2 ligands (HB1, CL), 1 pocket (best druggability 0.69). MolNFT v1…

PDB: 2BZH
Type: protein
Length: 275 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proto-oncogene serine threonine protein kinase PIM1
EC: 2.7.1.37
UniProt: P11309
Ligands: HB1, CL
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Proto-oncogene serine threonine protein kinase PIM1 (EC 2.7.1.37)	protein	275	39% helix, 23% strand	P11309

Ligands and binding sites

HB1 · Ruthenium-pyridocarbazole-1 · ligand · chains B
CL · Chloride ion · ion · chains B
EDO · 1,2-ethanediol · additive · chains B

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	348	0.69	0.82	43	HB1

Compared structures

2BZH · Crystal structure of the human PIM1 in complex with a ruthenium organometallic ligand RU1 · 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 2BZH · PDBe 2BZH · UniProt P11309

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