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Crystal structure of the JAK2 pseudokinase domain (mg-ATP-bound form)

Analyse Crystal structure of the JAK2 pseudokinase domain (mg-ATP-bound form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FVQ
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: ATP, MG
Pockets: 3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tyrosine-protein kinase JAK2 (EC 2.7.10.2)	protein	274	43% helix, 20% strand	O60674

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
ACT · Acetate ion · additive · 2 copies · 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	246	0.64	0.82	30	ATP, MG
2	95	0.39	0.76	12	ACT
3	60	0.38	0.79	17	empty

Compared structures

4FVQ · Crystal structure of the Jak2 pseudokinase domain (Mg-ATP-bound form) · 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 4FVQ · PDBe 4FVQ · UniProt O60674

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