Structure of PDB 4cqg Chain A

Receptor sequence
>4cqgA (length=313) Species: 10090 (Mus musculus) [Search protein sequence]
KDYDELLKYYELYETIGTGGFAKVKLACHVLTGEMVAIKIMDKNALGSDL
PRVKTEIDALKSLRHQHICQLYHVLETKNKIFMVLEYCPGGELFDYIISQ
DRLSEEETRVVFRQILSAVAYVHSQGYAHRDLKPENLLFDENHKLKLIDF
GLCAKCGSLAYAAPELIQGSEADVWSMGILLYVLMCGFLPFDDDNVMALY
KKIMRGKYEVPKWLSPSSILLLQQMLQVDPKKRISMRNLLNHPWVMQDYS
CPVEWQSKTPLTHLDEDCVTELSVHHRSSRQTMEDLISSWQYDHLTATYL
LLLAKKARLEHHH
3D structure
PDB4cqg The crystal structure of MPK38 in complex with OTSSP167, an orally administrative MELK selective inhibitor.
ChainA
Resolution2.57 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) D132 K134 E136 N137 D150 S171
Catalytic site (residue number reindexed from 1) D131 K133 E135 N136 D149 S158
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
2.7.11.1: non-specific serine/threonine protein 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 OT5 A I17 G18 V25 A38 K40 L86 E87 Y88 C89 E93 L139 I149 D150 I16 G17 V24 A37 K39 L85 E86 Y87 C88 E92 L138 I148 D149 PDBbind-CN: -logKd/Ki=9.39,IC50=0.41nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine 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:4cqg, PDBe:4cqg, PDBj:4cqg
PDBsum4cqg
PubMed24657156
UniProtQ61846|MELK_MOUSE Maternal embryonic leucine zipper kinase (Gene Name=Melk)

[Back to BioLiP]