MolNFT v2 · #156261 · protein

Crystal structure of Ser/Thr kinase Pim1 in complex with 10-DEBC derivatives

6L12 · Serine/threonine-protein kinase pim-1: “Crystal structure of Ser/Thr kinase Pim1 in complex with 10-DEBC derivatives”. X-ray diffraction at 1.87, 1 ligand (E2R), 2 pockets (best druggability 0.65). MolNFT v2 #156261 on GenesisL1: 3D…

PDB: 6L12
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.87
Source: Homo sapiens
Molecule: Serine/threonine-protein kinase pim-1
EC: 2.7.11.1
UniProt: P11309
Ligands: E2R
Pockets: 2 · best druggability 0.65

Structure

x-ray diffraction · resolution 1.87 · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Serine/threonine-protein kinase pim-1 (EC 2.7.11.1)	protein	273	40% helix, 23% strand	P11309

Ligands and binding sites

E2R · 4-[(2-chloranylphenoxazin-10-yl)methyl]cyclohexan-1-amine · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.65	0.83	25	E2R
2	121	0.49	0.80	26	empty

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

6L12 · Crystal structure of SER/THR kinase PIM1 in complex with 10-debc derivatives · 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 6L12 · PDBe 6L12 · UniProt P11309

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