Structure of PDB 5twl Chain A

Receptor sequence
>5twlA (length=319) Species: 9606 (Homo sapiens) [Search protein sequence]
GSKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGS
DLPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYII
SQDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLI
DFGLCGSLAYAAPELIQGKSYLGSEADVWSMGILLYVLMCGFLPFDDDNV
MALYKKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIM
QDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLT
ATYLLLLAKKARGKPVRLR
3D structure
PDB5twl MELK is not necessary for the proliferation of basal-like breast cancer cells.
ChainA
Resolution2.42 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) D133 K135 E137 N138 D151 S157
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 H91 A I17 K40 E57 C70 L86 E87 C89 E93 E136 L139 I149 D150 I18 K41 E58 C71 L87 E88 C90 E94 E137 L140 I150 D151 MOAD: ic50=10.5nM
PDBbind-CN: -logKd/Ki=7.98,IC50=10.5nM
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:5twl, PDBe:5twl, PDBj:5twl
PDBsum5twl
PubMed28926338
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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