Structure of PDB 3q32 Chain B

Receptor sequence
>3q32B (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
MRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHS
TEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSL
RDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENE
NRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDV
WSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGR
LPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAGH
3D structure
PDB3q32 Pyrrolo[1,2-f]triazines as JAK2 inhibitors: Achieving potency and selectivity for JAK2 over JAK3.
ChainB
Resolution2.5 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 A978 R980 N981 D994 S1016
Catalytic site (residue number reindexed from 1) D139 A141 R143 N144 D157 S179
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 J2I B L855 S862 V863 A880 K882 E930 Y931 L932 G935 R980 N981 L983 D994 L18 S25 V26 A43 K45 E93 Y94 L95 G98 R143 N144 L146 D157 MOAD: ic50=0.0018uM
BindingDB: IC50=1.8nM
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:3q32, PDBe:3q32, PDBj:3q32
PDBsum3q32
PubMed21282055
UniProtO60674|JAK2_HUMAN Tyrosine-protein kinase JAK2 (Gene Name=JAK2)

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