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Structural basis of JAK2 inhibition by the type II inhibtor nvp-BBT594

Analyse Structural basis of JAK2 inhibition by the type II inhibtor nvp-BBT594 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UGC
Type: protein
Length: 274 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tyrosine-protein kinase JAK2
EC: 2.7.10.2
UniProt: O60674
Ligands: 046
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase JAK2 (EC 2.7.10.2)	protein	274	47% helix, 17% strand	O60674

Ligands and binding sites

046 · 5-{[6-(acetylamino)pyrimidin-4-yl]oxy}-N-{4-[(4-methylpiperazin-1-yl)methyl]-3-(trifluoromethyl) phenyl}-2,3-dihydro-1H-indole-1-carboxamide · ligand · chains A
MLI · Malonate ion · additive · 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	507	0.73	0.82	51	046
2	65	0.33	0.76	20	empty

Compared structures

3UGC · Structural basis of Jak2 inhibition by the type II inhibtor NVP-BBT594 · 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 O60674
Elsewhere: RCSB PDB 3UGC · PDBe 3UGC · UniProt O60674

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