Structure of PDB 6khd Chain A

Receptor sequence
>6khdA (length=322) Species: 9606 (Homo sapiens) [Search protein sequence]
LICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDR
YCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLST
YDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQ
SDYTEERTLINPDIKVVDFGSATYDDEHHSTLVRHYRAPEVILALGWSQP
CDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKR
KYFHHDRLDWDEHSSAGRYVSRACKPLKEFMLSQDVEHERLFDLIQKMLE
YDPAKRITLREALKHPFFDLLK
3D structure
PDB6khd Structural Basis for the Selective Inhibition of Cdc2-Like Kinases by CX-4945.
ChainA
Resolution2.7 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
Catalytic site (residue number reindexed from 1) D140 K142 N145 D168
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 L19 G20 E21 F24 V27 A41 K43 F93 L96 L147 V167
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004712 protein serine/threonine/tyrosine kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004715 non-membrane spanning protein tyrosine kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0106310 protein serine kinase activity
Biological Process
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0043484 regulation of RNA splicing
Cellular Component
GO:0005634 nucleus

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6khd, PDBe:6khd, PDBj:6khd
PDBsum6khd
PubMed31531359
UniProtP49759|CLK1_HUMAN Dual specificity protein kinase CLK1 (Gene Name=CLK1)

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