Structure of PDB 4azf Chain A

Receptor sequence
>4azfA (length=407) Species: 9606 (Homo sapiens) [Search protein sequence]
HHHSSGVDLGTENLYFQSMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFS
YPEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKV
IGKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQD
KDNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRK
FAHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQ
RVYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDE
GDQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDVVLNG
GRSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQA
LRHPWLR
3D structure
PDB4azf Selectivity, Co-Crystal Structures and Neuroprotective Properties of Leucettines, a Family of Protein Kinase Inhibitors Derived from the Marine Sponge Alkaloid Leucettamine B.
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D275 K277 N280 D295 S312
Catalytic site (residue number reindexed from 1) D221 K223 N226 D241 S258
Enzyme Commision number 2.7.12.1: dual-specificity 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 3RA A G156 F160 V163 A176 K178 L230 L231 L282 I294 G102 F106 V109 A122 K124 L176 L177 L228 I240 PDBbind-CN: -logKd/Ki=6.35,Kd=450nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004712 protein serine/threonine/tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:4azf, PDBe:4azf, PDBj:4azf
PDBsum4azf
PubMed22998443
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

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