Structure of PDB 4fr4 Chain B

Receptor sequence
>4fr4B (length=350) Species: 9606 (Homo sapiens) [Search protein sequence]
ENEDVNFDHFEILRAIGKGSFGKVCIVQKNDTKKMYAMKYMNKQKCVERN
EVRNVFKELQIMQGLEHPFLVNLWYSFQDEEDMFMVVDLLLGGDLRYHLQ
QNVHFKEETVKLFICELVMALDYLQNQRIIHRDMKPDNILLDEHGHVHIT
DFNIAAMLPRETQITTMAGTKPYMAPEMFSSRKGAGYSFAVDWWSLGVTA
YELLRGRRPYHIRSSTSSKEIVHTFETTVVTYPSAWSQEMVSLLKKLLEP
NPDQRFSQLSDVQNFPYMNDINWDAVFQKRLIPGFIPNKGRLNCDPTFEL
EEMILESKKKEKDMRKCDSSQTCLLQEHLDSVQKEFIIFNREKVNRDFNK
3D structure
PDB4fr4 Crystal structure of human serine/threonine-protein kinase 32A (YANK1)
ChainB
Resolution2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D146 K148 D150 N151 D164 T183
Catalytic site (residue number reindexed from 1) D133 K135 D137 N138 D151 T170
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 STU B I29 A50 K52 V84 L102 L103 G106 D107 D150 L153 T163 L305 I16 A37 K39 V71 L89 L90 G93 D94 D137 L140 T150 L292
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
GO:0044024 histone H2AS1 kinase activity
GO:0046872 metal ion binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0035556 intracellular signal transduction
Cellular Component
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4fr4, PDBe:4fr4, PDBj:4fr4
PDBsum4fr4
PubMed
UniProtQ8WU08|ST32A_HUMAN Serine/threonine-protein kinase 32A (Gene Name=STK32A)

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