Structure of PDB 5eak Chain B

Receptor sequence
>5eakB (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
GNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFRE
VRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEK
EARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFCGSP
PYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL
RGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDEL
KPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGY
3D structure
PDB5eak Optimization of microtubule affinity regulating kinase (MARK) inhibitors with improved physical properties.
ChainB
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) D175 K177 E179 N180 D193 S212
Catalytic site (residue number reindexed from 1) D125 K127 E129 N130 D143 S149
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
2.7.11.26: [tau 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 24R B I59 K61 V67 K82 M129 Y131 A132 G135 E179 L182 D193 I9 K11 V17 K32 M79 Y81 A82 G85 E129 L132 D143
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
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Biological Process
External links
PDB RCSB:5eak, PDBe:5eak, PDBj:5eak
PDBsum5eak
PubMed27491711
UniProtQ7KZI7|MARK2_HUMAN Serine/threonine-protein kinase MARK2 (Gene Name=MARK2)

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