Structure of PDB 5iha Chain A

Receptor sequence
>5ihaA (length=303) Species: 9606 (Homo sapiens) [Search protein sequence]
MDYDELLKYYELHETIGAKVKLACHILTGEMVAIKIMDKNTLRIKTEIEA
LKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEETR
VVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAKSLAY
AAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRG
KYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQ
SKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKK
ARG
3D structure
PDB5iha Toward the Validation of Maternal Embryonic Leucine Zipper Kinase: Discovery, Optimization of Highly Potent and Selective Inhibitors, and Preliminary Biology Insight.
ChainA
Resolution1.96 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D132 K134 E136 N137 D150 S171
Catalytic site (residue number reindexed from 1) D122 K124 E126 N127 D140 S147
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 6BE A I17 L27 A38 Y88 C89 P90 L139 I149 I16 L22 A33 Y78 C79 P80 L129 I139 MOAD: ic50=0.41uM
PDBbind-CN: -logKd/Ki=8.05,IC50=0.009uM
BindingDB: IC50=410nM
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:5iha, PDBe:5iha, PDBj:5iha
PDBsum5iha
PubMed27187609
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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