Structure of PDB 2qlq Chain A

Receptor sequence
>2qlqA (length=245) Species: 9031 (Gallus gallus) [Search protein sequence]
AKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLAQVMKKLR
HEKLVQLYAVVSEPIYIVTEYMSKGCLLDFLKGEMGKYLRLPQLVDMAAQ
IASGMAYVERMNYVHRDLRAANILVGENLVCKVADFPIKWTAPEAALYGR
FTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECP
ESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
3D structure
PDB2qlq Structural insights into how irreversible inhibitors can overcome drug resistance in EGFR.
ChainA
Resolution2.33 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D386 R388 A390 N391 D404
Catalytic site (residue number reindexed from 1) D117 R119 A121 N122 D135
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine 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 SR2 A V281 A293 K295 T338 M341 C345 D348 L393 D404 V26 A38 K40 T69 M72 C76 D79 L124 D135 PDBbind-CN: -logKd/Ki=6.63,IC50=236nM
BindingDB: IC50=>27000nM
BS02 SR2 A C483 P484 E486 C487 E489 C195 P196 E198 C199 E201 PDBbind-CN: -logKd/Ki=6.63,IC50=236nM
BindingDB: IC50=>27000nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine 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:2qlq, PDBe:2qlq, PDBj:2qlq
PDBsum2qlq
PubMed18316192
UniProtP00523|SRC_CHICK Proto-oncogene tyrosine-protein kinase Src (Gene Name=SRC)

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