Structure of PDB 4yps Chain A

Receptor sequence
>4ypsA (length=280) Species: 9606 (Homo sapiens) [Search protein sequence]
GSGIRVHHIKRRDIVLKWELGEGKVFLAECHNLLDKMLVAVKALSESARQ
DFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHG
PDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRN
CLVGQGLVVKIGDMSRDIYSTDYYRVTMLPIRWMPPESILYRKFTTESDV
WSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIM
RGCWQREPQQRHSIKDVHARLQALAQAPPV
3D structure
PDB4yps (R)-2-Phenylpyrrolidine Substituted Imidazopyridazines: A New Class of Potent and Selective Pan-TRK Inhibitors.
ChainA
Resolution2.1012 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D650 A652 R654 N655 D668 S677 L689
Catalytic site (residue number reindexed from 1) D145 A147 R149 N150 D163 S170 L179
Enzyme Commision number 2.7.10.1: receptor 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 4F6 A L516 G517 V524 A542 F589 M592 R654 L657 L20 G21 V25 A40 F84 M87 R149 L152 PDBbind-CN: -logKd/Ki=7.12,IC50=0.075uM
BindingDB: IC50=75nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0004714 transmembrane receptor protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4yps, PDBe:4yps, PDBj:4yps
PDBsum4yps
PubMed26005534
UniProtP04629|NTRK1_HUMAN High affinity nerve growth factor receptor (Gene Name=NTRK1)

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