Structure of PDB 5sys Chain A

Receptor sequence
>5sysA (length=258) Species: 9031 (Gallus gallus) [Search protein sequence]
DAWEIPRESLRLEVKLGQGCFGECWMGTWNGTTRVAIKTLKPGTMSPEAF
LQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKY
LRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGP
IKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQV
ERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEP
QYQPGENL
3D structure
PDB5sys A combined approach reveals a regulatory mechanism coupling Src's kinase activity, localization, and phosphotransferase-independent functions
ChainA
Resolution2.8 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
Catalytic site (residue number reindexed from 1) D129 R131 A133 N134 D147
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 72F A C281 A293 K295 E310 M314 L322 I336 T338 Y340 M341 H384 A403 D404 F405 C24 A36 K38 E53 M57 L65 I79 T81 Y83 M84 H127 A146 D147 F148
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:5sys, PDBe:5sys, PDBj:5sys
PDBsum5sys
PubMed
UniProtP00523|SRC_CHICK Proto-oncogene tyrosine-protein kinase Src (Gene Name=SRC)

[Back to BioLiP]