Structure of PDB 3iec Chain D

Receptor sequence
>3iecD (length=311) Species: 9606 (Homo sapiens) [Search protein sequence]
HIGNYRLLKTIGAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVR
IMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGWMKEKEA
RAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTF
GNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG
QNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDR
WMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYN
EVMATYLLLGY
3D structure
PDB3iec Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates.
ChainD
Resolution2.2 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) D123 K125 E127 N128 D141 S160
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 peptide D E136 F138 D139 D175 E179 D193 F196 F209 C210 G211 P214 F221 S247 L248 P249 D251 K256 R261 E84 F86 D87 D123 E127 D141 F144 F157 C158 G159 P162 F169 S195 L196 P197 D199 K204 R209
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:3iec, PDBe:3iec, PDBj:3iec
PDBsum3iec
PubMed19966800
UniProtQ7KZI7|MARK2_HUMAN Serine/threonine-protein kinase MARK2 (Gene Name=MARK2)

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