Structure of PDB 5y80 Chain A

Receptor sequence
>5y80A (length=306) Species: 9606 (Homo sapiens) [Search protein sequence]
SQSDFVGQTVELGELRLRVRRVLAEGGFAFVYEAQDVGSGREYALKRLLS
NEEEKNRAIIQEVCFMKKLSGHPNIVQFCSAASIGKEESDTGQAEFLLLT
ELCKGQLVEFLKKMGPLSCDTVLKIFYQTCRAVQHMHRQKPPIIHRDLKV
ENLLLSNQGTIKLCDFGSATTISHYPDYSWSAQRRALVEEEITRNTTPMY
RTPEIIDLYSNFPIGEKQDIWALGCILYLLCFRQHPFEDGAKLRIVNGKY
SIPPHDTQYTVFHSLIRAMLQVNPEERLSIAEVVHQLQEIAAARNVNPKS
PITELL
3D structure
PDB5y80 Structural Basis for the Inhibition of Cyclin G-Associated Kinase by Gefitinib.
ChainA
Resolution2.5 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) D173 K175 N178 D191 T223
Catalytic site (residue number reindexed from 1) D147 K149 N152 D165 T197
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 IRE A L46 K69 C126 G128 Q129 L180 L23 K46 C103 G105 Q106 L154 MOAD: Kd=1.62nM
PDBbind-CN: -logKd/Ki=8.79,Kd=1.62nM
BS02 IRE A A81 R172 G193 S194 H200 V214 I218 N221 Q244 A58 R146 G167 S168 H174 V188 I192 N195 Q218 MOAD: Kd=1.62nM
PDBbind-CN: -logKd/Ki=8.79,Kd=1.62nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:5y80, PDBe:5y80, PDBj:5y80
PDBsum5y80
PubMed30214852
UniProtO14976|GAK_HUMAN Cyclin-G-associated kinase (Gene Name=GAK)

[Back to BioLiP]