Structure of PDB 4d2p Chain B

Receptor sequence
>4d2pB (length=323) Species: 9606 (Homo sapiens) [Search protein sequence]
MKDYDELLKYYELHETIGTGGFAKVKLACHILTGEMVAIKIMDKNTLGSD
LPRIKTEIEALKNLRHQHICQLYHVLETANKIFMVLEYCPGGELFDYIIS
QDRLSEEETRVVFRQIVSAVAYVHSQGYAHRDLKPENLLFDEYHKLKLID
FGLCAKPKGNKDCGALAYAAPELIQGGSEADVWSMGILLYVLMCGFLPFD
DDTAAALVAKIMRGKYDVPKWLSPSSILLLQQMLQVDPKKRISMKNLLNH
PWIMQDYNYPVEWQSKNPFIHLDDDCVTELSVHHRNNRQTMEDLISLWQY
DHLTATYLLLLAKKARGKPVRLR
3D structure
PDB4d2p Fragment-Based Discovery of Type I Inhibitors of Maternal Embryonic Leucine Zipper Kinase
ChainB
Resolution2.55 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) D132 K134 E136 N137 D150 A165
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 6Z7 B L27 A38 K40 E57 L61 C70 Y88 C89 P90 L139 I149 D150 L27 A38 K40 E57 L61 C70 Y88 C89 P90 L139 I149 D150 PDBbind-CN: -logKd/Ki=5.68,IC50=2.1uM
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:4d2p, PDBe:4d2p, PDBj:4d2p
PDBsum4d2p
PubMed25589925
UniProtQ14680|MELK_HUMAN Maternal embryonic leucine zipper kinase (Gene Name=MELK)

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