Structure of PDB 7uy0 Chain A

Receptor sequence
>7uy0A (length=448) Species: 9606 (Homo sapiens) [Search protein sequence]
TLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIP
SNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGA
YSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEV
NDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWL
GTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQLYAVVSEEP
IYIVTEFMCHGSLLDFLKNPEGQDLRLPQLVDMAAQVAEGMAYMERMNYI
HRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKFPIKWTAPEA
ALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPC
PPGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYEEIP
3D structure
PDB7uy0 ATP-site inhibitors induce unique conformations of the acute myeloid leukemia-associated Src-family kinase, Fgr.
ChainA
Resolution2.55 Å
3D
structure
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Enzymatic activity
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 VSE A V281 A293 K295 M314 V323 I336 T338 F340 M341 S345 D348 L393 D404 F405 V198 A210 K212 M231 V240 I253 T255 F257 M258 S262 D265 L310 D321 F322
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:7uy0, PDBe:7uy0, PDBj:7uy0
PDBsum7uy0
PubMed36115344
UniProtP09769|FGR_HUMAN Tyrosine-protein kinase Fgr (Gene Name=FGR)

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