Structure of PDB 2yab Chain A

Receptor sequence
>2yabA (length=299) Species: 10090 (Mus musculus) [Search protein sequence]
TFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAS
RRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELF
DFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNI
PIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWS
IGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFI
RKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYV
3D structure
PDB2yab Structure of the Dimeric Autoinhibited Conformation of Dapk2, a Pro-Apoptotic Protein Kinase.
ChainA
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) D139 K141 E143 N144 D161 T180
Catalytic site (residue number reindexed from 1) D137 K139 E141 N142 D159 T178
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 AMP A G20 S21 V27 A40 K42 V96 I160 D161 G18 S19 V25 A38 K40 V94 I158 D159
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005516 calmodulin binding
GO:0005524 ATP binding
GO:0044024 histone H2AS1 kinase activity
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0006915 apoptotic process
GO:0016310 phosphorylation
GO:0035556 intracellular signal transduction
GO:1990266 neutrophil migration
GO:2001242 regulation of intrinsic apoptotic signaling pathway
Cellular Component
GO:0005737 cytoplasm
GO:0031410 cytoplasmic vesicle
GO:0034423 autophagosome lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2yab, PDBe:2yab, PDBj:2yab
PDBsum2yab
PubMed21497605
UniProtQ8VDF3|DAPK2_MOUSE Death-associated protein kinase 2 (Gene Name=Dapk2)

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