Structure of PDB 4nct Chain A

Receptor sequence

>4nctA (length=342) Species: 9606 (Homo sapiens)

KVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQE
WVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNH
LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSI
IHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVL
LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH
ILDQAPKARKFFEKLPDGTWNLKKTEYKPPGTRKLHNILGVETGGPGGRR
AGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK

3D structure

• PDB: 4nct The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine.
• Chain: A
• Resolution: 2.597 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D287 K289 N292 D307 S324
• Catalytic site (residue number reindexed from 1): D154 K156 N159 D174 S191
• 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	2K2	A	I165 G166 V173 A186 M240 E291 D307	I32 G33 V40 A53 M107 E158 D174	PDBbind-CN: -logKd/Ki=7.55,Ki=28.4nM BindingDB: Kd=100nM

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:4nct, PDBe:4nct, PDBj:4nct
• PDBsum: 4nct
• PubMed: 25945585
• UniProt: Q13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)