Structure of PDB 6i5i Chain A

Receptor sequence
>6i5iA (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
SMHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKN
VDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLG
LSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENIL
FVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHY
RAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERIL
GPLPKHMIQKTRKRKYFRLDWDEHSSAGRYVSRACKPLKEFMLSQDVEHE
RLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKS
3D structure
PDB6i5i Furo[3,2-b]pyridine: A Privileged Scaffold for Highly Selective Kinase Inhibitors and Effective Modulators of the Hedgehog Pathway.
ChainA
Resolution1.6 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) D143 K145 N148 D180 T197
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 H3E A L167 G168 F172 V175 A189 K191 F241 L244 E292 L295 V324 L22 G23 F27 V30 A44 K46 F96 L99 E147 L150 V179 PDBbind-CN: -logKd/Ki=8.05,IC50=9nM
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:6i5i, PDBe:6i5i, PDBj:6i5i
PDBsum6i5i
PubMed30569600
UniProtP49759|CLK1_HUMAN Dual specificity protein kinase CLK1 (Gene Name=CLK1)

[Back to BioLiP]