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Crystal structure of JAK2 kinase domain in complex with compound 30

Analyse Crystal structure of JAK2 kinase domain in complex with compound 30 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UYW
Type: protein
Length: 290 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: OV0
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase JAK2 (EC 2.7.10.2)	protein	290	41% helix, 19% strand	O60674

Ligands and binding sites

OV0 · 2-(2,6-difluorophenyl)-4-[4-(pyrrolidine-1-carbonyl) anilino]-5H-pyrrolo[3,4-b]pyridin-5-one · ligand · chains A

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	336	0.66	0.81	51	OV0
2	93	0.41	0.78	21	empty
3	65	0.29	0.74	18	empty

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

7UYW · Crystal structure of JAK2 kinase domain in complex with compound 30 · 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 7UYW · PDBe 7UYW · UniProt O60674

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