Structure of PDB 6vni Chain A

Receptor sequence
>6vniA (length=291) Species: 9606 (Homo sapiens) [Search protein sequence]
TQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEH
LRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYL
QKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVK
IGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFG
VVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRP
DGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
3D structure
PDB6vni Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof.
ChainA
Resolution2.1 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) D135 R139 N140 D153
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 R61 A L855 G856 V863 A880 M929 Y931 L932 G935 L983 D994 L14 G15 V22 A39 M88 Y90 L91 G94 L142 D153
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:6vni, PDBe:6vni, PDBj:6vni
PDBsum6vni
PubMed33570945
UniProtO60674|JAK2_HUMAN Tyrosine-protein kinase JAK2 (Gene Name=JAK2)

[Back to BioLiP]