Structure of PDB 6vnf Chain A

Receptor sequence
>6vnfA (length=298) Species: 9606 (Homo sapiens) [Search protein sequence]
LYFQGDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKL
QHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPY
GSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILV
ENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVA
SDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKN
NGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
3D structure
PDB6vnf Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.
ChainA
Resolution2.06 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D976 R980 N981 D994
Catalytic site (residue number reindexed from 1) D142 R146 N147 D160
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 R6S A L855 G856 K857 G858 V863 A880 M929 L932 G935 N981 L983 D994 L21 G22 K23 G24 V29 A46 M95 L98 G101 N147 L149 D160
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6vnf, PDBe:6vnf, PDBj:6vnf
PDBsum6vnf
PubMed33570945
UniProtO60674|JAK2_HUMAN Tyrosine-protein kinase JAK2 (Gene Name=JAK2)

[Back to BioLiP]