Structure of PDB 2src Chain A

Receptor sequence
>2srcA (length=450) Species: 9606 (Homo sapiens) [Search protein sequence]
TTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIP
SNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGA
YCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKH
ADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWM
GTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP
IYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYV
HRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEA
ALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPC
PPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
3D structure
PDB2src Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
ChainA
Resolution1.5 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 F424
Catalytic site (residue number reindexed from 1) D303 R305 A307 N308 D321 F341
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 ANP A L273 G276 V281 A293 K295 Y340 M341 R388 L393 L190 G193 V198 A210 K212 Y257 M258 R305 L310
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:2src, PDBe:2src, PDBj:2src
PDBsum2src
PubMed10360179
UniProtP12931|SRC_HUMAN Proto-oncogene tyrosine-protein kinase Src (Gene Name=SRC)

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