Structure of PDB 6fyo Chain A

Receptor sequence
>6fyoA (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
HLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVD
RYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLS
TYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFV
QSDYTEAYNKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEV
ILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPK
HMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRRCKPLKEFMLSQDVEHERL
FDLIQKMLEYDPAKRITLREALKHPFFDLLK
3D structure
PDB6fyo X-ray Structures and Feasibility Assessment of CLK2 Inhibitors for Phelan-McDermid Syndrome.
ChainA
Resolution2.32 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) D141 K143 N146 D175 T192
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 EAQ A L167 A189 K191 F241 L244 G245 L246 L295 V324 D325 L20 A42 K44 F94 L97 G98 L99 L148 V174 D175
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:6fyo, PDBe:6fyo, PDBj:6fyo
PDBsum6fyo
PubMed29985556
UniProtP49759|CLK1_HUMAN Dual specificity protein kinase CLK1 (Gene Name=CLK1)

[Back to BioLiP]