Structure of PDB 5l4q Chain B

Receptor sequence
>5l4qB (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
GYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEH
DLQVCKREIQIMRDLSGHKNIVGYIDSSINNVVWEVLILMDFCRGGQVVN
LMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHD
RGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSG
KIITTKADIWALGCLLYKLCYFTLPFNFTIPDNSRYSQDMHCLIRYMLEP
DPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKL
3D structure
PDB5l4q Synthesis and Structure-Activity Relationships of 3,5-Disubstituted-pyrrolo[2,3- b]pyridines as Inhibitors of Adaptor-Associated Kinase 1 with Antiviral Activity.
ChainB
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D176 K178 N181 D194 T222
Catalytic site (residue number reindexed from 1) D140 K142 N145 D158 T186
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 LKB B A72 K74 V104 M126 D127 F128 C129 G132 N136 L183 D194 A40 K42 V72 M90 D91 F92 C93 G96 N100 L147 D158 BindingDB: Kd=53nM,Ki=541nM,IC50=1170nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:5l4q, PDBe:5l4q, PDBj:5l4q
PDBsum5l4q
PubMed31136173
UniProtQ2M2I8|AAK1_HUMAN AP2-associated protein kinase 1 (Gene Name=AAK1)

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