Structure of PDB 5es1 Chain A

Receptor sequence
>5es1A (length=304) Species: 9606 (Homo sapiens) [Search protein sequence]
PHVGNYRLLRTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPSSLQKL
FREVRIMKGLNHPNIVKLFEVIETEKTLYLVMEYASAGEVFDYLVSHGRM
KEKEARAKFRQIVSAVHYCHQKNIVHRDLKAENLLLDAEANIKIADFGFS
NSPPYAAPELFQGKKYDGPEVDIWSLGVILYTLVSGSLPFDGHNLKELRE
RVLRGKYRVPFYMSTDCESILRRFLVLNPAKRCTLEQIMKDKWINIGYEG
EELKPYTEPEEDFGDTKRIEVMVGMGYTREEIKESLTSQKYNEVTATYLL
LGRK
3D structure
PDB5es1 Crystal structure of microtubule affinity-regulating kinase 4 catalytic domain in complex with a pyrazolopyrimidine inhibitor.
ChainA
Resolution2.8 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) D178 K180 E182 N183 D196 S215
Catalytic site (residue number reindexed from 1) D128 K130 E132 N133 D146 S152
Enzyme Commision number 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 5RC A G65 V70 A83 K85 M132 Y134 A135 G138 E182 D196 G15 V20 A33 K35 M82 Y84 A85 G88 E132 D146 PDBbind-CN: -logKd/Ki=8.34,IC50=4.6nM
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:5es1, PDBe:5es1, PDBj:5es1
PDBsum5es1
PubMed26841763
UniProtQ96L34|MARK4_HUMAN MAP/microtubule affinity-regulating kinase 4 (Gene Name=MARK4)

[Back to BioLiP]