Structure of PDB 4umu Chain A

Receptor sequence
>4umuA (length=316) Species: 9606 (Homo sapiens) [Search protein sequence]
DYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDLP
RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQD
RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG
LCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDTAAAL
VAKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDY
NYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATY
LLLLAKKARGKPVRLR
3D structure
PDB4umu Structure-Based Design of Type II Inhibitors Applied to Maternal Embryonic Leucine Zipper Kinase.
ChainA
Resolution2.02 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) D130 K132 E134 N135 D148 S154
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 0V0 A A38 E57 L61 I69 C89 L139 L148 I149 D150 F151 A36 E55 L59 I67 C87 L137 L146 I147 D148 F149 PDBbind-CN: -logKd/Ki=6.19,IC50=0.65uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4umu, PDBe:4umu, PDBj:4umu
PDBsum4umu
PubMed25589926
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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