Structure of PDB 5k00 Chain A

Receptor sequence
>5k00A (length=311) Species: 9606 (Homo sapiens) [Search protein sequence]
MDYDELLKYYELHETIGTGAKVKLACHILTGEMVAIKIMDKNTLGSDLPR
IKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDR
LSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGL
CAKPSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNVMA
LYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQD
YNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTAT
YLLLLAKKARG
3D structure
PDB5k00 Addition" and "Subtraction": Selectivity Design for Type II Maternal Embryonic Leucine Zipper Kinase Inhibitors.
ChainA
Resolution1.77 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) D129 K131 E133 N134 D147 S155
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 6PV A A38 K40 L61 L64 C70 L86 Y88 C89 G92 E93 L139 I149 D150 F151 A35 K37 L58 L61 C67 L83 Y85 C86 G89 E90 L136 I146 D147 F148 MOAD: ic50=7nM
PDBbind-CN: -logKd/Ki=8.15,IC50=7nM
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:5k00, PDBe:5k00, PDBj:5k00
PDBsum5k00
PubMed28186750
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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