Structure of PDB 4aze Chain A

Receptor sequence

>4azeA (length=350) Species: 9606 (Homo sapiens)

ERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVE
QEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFR
NHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPEL
SIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPE
VLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP
AHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVET
GGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK

3D structure

• PDB: 4aze Selectivity, Co-Crystal Structures and Neuroprotective Properties of Leucettines, a Family of Protein Kinase Inhibitors Derived from the Marine Sponge Alkaloid Leucettamine B.
• Chain: A
• Resolution: 3.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D287 K289 N292 D307 S324
• Catalytic site (residue number reindexed from 1): D156 K158 N161 D176 S193
• Enzyme Commision number: 2.7.11.23: [RNA-polymerase]-subunit kinase.
  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	I165 F170 A186 K188 L241 L294 D307	I34 F39 A55 K57 L110 L163 D176	PDBbind-CN: -logKd/Ki=8.11,Kd=7.8nM BindingDB: IC50=7.6nM

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
• GO:0046777 protein autophosphorylation

External links

• PDB: RCSB:4aze, PDBe:4aze, PDBj:4aze
• PDBsum: 4aze
• PubMed: 22998443
• UniProt: Q13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)