Structure of PDB 5maf Chain A

Receptor sequence
>5mafA (length=315) Species: 9606 (Homo sapiens) [Search protein sequence]
PKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLDLP
RIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIISQD
RLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLIDFG
LCAKSLAYAAPELIQGKLGSEADVWSMGILLYVLMCGFLPFDDDNVMALY
KKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNHPWIMQDYN
YPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQYDHLTATYL
LLLAKKARGKPVRLR
3D structure
PDB5maf The target landscape of clinical kinase drugs.
ChainA
Resolution2.8 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 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 XIN A I17 G18 V25 A38 K40 L86 Y88 C89 G92 L139 I149 D150 I17 G18 V25 A38 K40 L84 Y86 C87 G90 L137 I147 D148 BindingDB: Kd=4.9nM,Ki=5.6nM,IC50=43.0nM
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:5maf, PDBe:5maf, PDBj:5maf
PDBsum5maf
PubMed29191878
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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