Structure of PDB 5tx3 Chain A

Receptor sequence
>5tx3A (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
SGSMKDYDELLKYYELHETIGTAKVKLACHILTGEMVAIKIMDKNIKTEI
EALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQDRLSEEE
TRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFGLGSLAY
AAPELIQGKGSEADVWSMGILLYVLMCGFLPFDDDNVMALYKKIMRGKYD
VPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYNYPVEWQSKN
PFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYLLLLAKKARG
KPVRLR
3D structure
PDB5tx3 MELK is not necessary for the proliferation of basal-like breast cancer cells.
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D132 K134 E136 N137 D150 S171
Catalytic site (residue number reindexed from 1) D124 K126 E128 N129 D142 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 7MY A V25 K40 Y88 C89 E93 L139 I149 V25 K40 Y80 C81 E85 L131 I141 PDBbind-CN: -logKd/Ki=8.85,IC50~1.4nM
BS02 7MY A E15 T16 E18 T19 PDBbind-CN: -logKd/Ki=8.85,IC50~1.4nM
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:5tx3, PDBe:5tx3, PDBj:5tx3
PDBsum5tx3
PubMed28926338
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

[Back to BioLiP]