Structure of PDB 6yte Chain C

Receptor sequence
>6yteC (length=338) Species: 9606 (Homo sapiens) [Search protein sequence]
MHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNV
DRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGL
STYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILF
VQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYR
APEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILG
PLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRACKPLKEFMLSQDVE
HERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI
3D structure
PDB6yte DFG-1 Residue Controls Inhibitor Binding Mode and Affinity, Providing a Basis for Rational Design of Kinase Inhibitor Selectivity.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D288 K290 N293 D325 T342
Catalytic site (residue number reindexed from 1) D142 K144 N147 D179 T196
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 EAE C V175 A189 K191 F241 L244 L295 D325 V29 A43 K45 F95 L98 L149 D179 MOAD: Kd=0.075uM
BindingDB: Kd=19nM,IC50=49nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6yte, PDBe:6yte, PDBj:6yte
PDBsum6yte
PubMed32787076
UniProtP49759|CLK1_HUMAN Dual specificity protein kinase CLK1 (Gene Name=CLK1)

[Back to BioLiP]