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High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to PN5-114.

Analyse High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LL4
Type: protein
Length: 297 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: Y5D
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase JAK2 (EC 2.7.10.2)	protein	297	44% helix, 18% strand	O60674

Ligands and binding sites

Y5D · {1-(ethylsulfonyl)-3-[4-(2-{[3-fluoro-4-(1-methylpiperidin-4-yl)phenyl]amino}-7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1H-pyrazol-1-yl]azetidin-3-yl}acetonitrile · ligand · chains A

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	562	0.72	0.80	51	Y5D

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

7LL4 · High-resolution crystal structure of human JAK2 kinase domain (JH1) bound to PN5-114. · the same entry in another collection · chain A against A, TM-score 1.00

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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 7LL4 · PDBe 7LL4 · UniProt O60674

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