Structure of PDB 1yvj Chain A

Receptor sequence
>1yvjA (length=290) Species: 9606 (Homo sapiens) [Search protein sequence]
PTIFEERHLKYISQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQHSGPD
QQRDFQREIQILKALHSDFIVKYRGVSYGPGRPELRLVMEYLPSGCLRDF
LQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHV
KIADFGLAKLLPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSF
GVVLYELFTYCDKSCSPSAEFLRMMGCERDVPALCRLLELLEEGQRLPAP
PACPAEVHELMKLCWAPSPQDRPSFSALGPQLDMLWSGSR
3D structure
PDB1yvj Crystal structure of the Jak3 kinase domain in complex with a staurosporine analog
ChainA
Resolution2.55 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) D949 A951 R953 N954 D967
Catalytic site (residue number reindexed from 1) D136 A138 R140 N141 D154
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 4ST A L828 G829 V836 A853 M902 Y904 L905 G908 R911 R953 L956 D967 L15 G16 V23 A40 M89 Y91 L92 G95 R98 R140 L143 D154
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:1yvj, PDBe:1yvj, PDBj:1yvj
PDBsum1yvj
PubMed15831699
UniProtP52333|JAK3_HUMAN Tyrosine-protein kinase JAK3 (Gene Name=JAK3)

[Back to BioLiP]