Structure of PDB 4bkz Chain A

Receptor sequence
>4bkzA (length=309) Species: 9606 (Homo sapiens) [Search protein sequence]
KDYDELLKYYELHETIGTGAKVKLACHILTGEMVAIKIMDKNTLLPRIKT
EIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSE
EETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLCAS
LAYAAPELIQGGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGK
YDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQS
KNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKA
RGKPVRLRL
3D structure
PDB4bkz Structural Insight Into Maternal Embryonic Leucine Zipper Kinase (Melk) Conformation and Inhibition Towards Structure- Based Drug Design.
ChainA
Resolution2.2 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) D126 K128 E130 N131 D144 S150
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 1WS A I17 A38 L86 E87 Y88 C89 P90 N137 L139 I149 I16 A35 L80 E81 Y82 C83 P84 N131 L133 I143 MOAD: ic50=0.027uM
PDBbind-CN: -logKd/Ki=7.57,IC50=0.027uM
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:4bkz, PDBe:4bkz, PDBj:4bkz
PDBsum4bkz
PubMed23914841
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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