Structure of PDB 4d2v Chain B

Receptor sequence
>4d2vB (length=322) Species: 9606 (Homo sapiens) [Search protein sequence]
KDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSDL
PRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQ
DRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDF
GLCAKPKGNKDCGALAYAAPELIQGGSEADVWSMGILLYVLMCGFLPFDD
DTAAALVAKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHP
WIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYD
HLTATYLLLLAKKARGKPVRLR
3D structure
PDB4d2v Fragment-Based Discovery of Type I Inhibitors of Maternal Embryonic Leucine Zipper Kinase
ChainB
Resolution2.45 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 A171
Catalytic site (residue number reindexed from 1) D131 K133 E135 N136 D149 A164
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 45R B I17 L27 K40 E57 L86 C89 P90 I149 D150 I16 L26 K39 E56 L85 C88 P89 I148 D149 PDBbind-CN: -logKd/Ki=7.43,IC50=0.037uM
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
View graph for
Biological Process
External links
PDB RCSB:4d2v, PDBe:4d2v, PDBj:4d2v
PDBsum4d2v
PubMed25589925
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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