Structure of PDB 5d11 Chain A

Receptor sequence
>5d11A (length=254) Species: 9031 (Gallus gallus) [Search protein sequence]
DAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSEAQV
MKKLRHEKLVQLYAVVSEEPIYIVMEYMSKGCLLDFLKGEMGKYLRLPQL
VDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLFPIKWT
APEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGY
RMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPQYQP
GENL
3D structure
PDB5d11 Targeting Drug Resistance in EGFR with Covalent Inhibitors: A Structure-Based Design Approach.
ChainA
Resolution2.3 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) D386 R388 A390 N391 D404 F424
Catalytic site (residue number reindexed from 1) D123 R125 A127 N128 D141 F145
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 56G A L273 G274 A293 E339 Y340 M341 S342 G344 C345 L393 L16 G17 A36 E76 Y77 M78 S79 G81 C82 L130 PDBbind-CN: -logKd/Ki=7.55,IC50=0.028uM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5d11, PDBe:5d11, PDBj:5d11
PDBsum5d11
PubMed26275028
UniProtP00523|SRC_CHICK Proto-oncogene tyrosine-protein kinase Src (Gene Name=SRC)

[Back to BioLiP]