Structure of PDB 6fyv Chain A

Receptor sequence
>6fyvA (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
ICQSGDVLRARYEIVDTLGEGAFGKVVECIDHGMDGMHVAVKIVKNVGRY
REAARSEIQVLEHLNSTDPNSVFRCVQMLEWFDHHGHVCIVFELLGLSTY
DFIKENSFLPFQIDHIRQMAYQICQSINFLHHNKLTHTDLKPENILFVKS
DYVVKYNKRDERTLKNTDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVIL
ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPIPQHM
IQKTRKRKYFHHNQLDWDEHSSAGRYVRRRCKPLKEFMLCHDEEHEKLFD
LVRRMLEYDPTQRITLDEALQHPFFDLLK
3D structure
PDB6fyv X-ray Structures and Feasibility Assessment of CLK2 Inhibitors for Phelan-McDermid Syndrome.
ChainA
Resolution2.46 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D288 K290 N293 D325 T342
Catalytic site (residue number reindexed from 1) D139 K141 N144 D173 T190
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 3NG A L167 G168 E169 F172 V175 A189 K191 F241 L244 L295 V324 D325 L18 G19 E20 F23 V26 A40 K42 F92 L95 L146 V172 D173 MOAD: ic50=11nM
PDBbind-CN: -logKd/Ki=7.96,IC50=11nM
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:6fyv, PDBe:6fyv, PDBj:6fyv
PDBsum6fyv
PubMed29985556
UniProtQ9HAZ1|CLK4_HUMAN Dual specificity protein kinase CLK4 (Gene Name=CLK4)

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