Structure of PDB 4aze Chain B

Receptor sequence

>4azeB (length=347) Species: 9606 (Homo sapiens)

VYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEW
VAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHL
CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSII
HCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLL
GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI
LDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGP
GGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK

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: B
• 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): D153 K155 N158 D173 S190
• 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	peptide	B	E366 V367 K393	E232 V233 K259
BS02	3RA	B	F170 A186 K188 L241 N244 L294 D307	F36 A52 K54 L107 N110 L160 D173	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)