Structure of PDB 6vgl Chain D

Receptor sequence
>6vglD (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
QFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHL
RDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQ
KHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKI
GDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGV
VLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPD
GCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMA
3D structure
PDB6vgl Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.
ChainD
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D976 R980 N981 D994
Catalytic site (residue number reindexed from 1) D134 R138 N139 D152
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 RXT D L855 A880 V911 M929 E930 L932 R980 N981 L983 G993 D994 L13 A38 V69 M87 E88 L90 R138 N139 L141 G151 D152 BindingDB: IC50=2.8nM,EC50=12nM,Kd=0.036000nM,Ki=0.100000nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6vgl, PDBe:6vgl, PDBj:6vgl
PDBsum6vgl
PubMed33570945
UniProtO60674|JAK2_HUMAN Tyrosine-protein kinase JAK2 (Gene Name=JAK2)

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