Structure of PDB 4at4 Chain A

Receptor sequence
>4at4A (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
GAMDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCKILVAVKTLKDA
SDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNK
FLRAHGPDAVLMAPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATR
NCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKF
TTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQ
EVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG
3D structure
PDB4at4 The Crystal Structures of Trka and Trkb Suggest Key Regions for Achieving Selective Inhibition.
ChainA
Resolution2.36 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D692 A694 R696 N697 D710 S719 L731
Catalytic site (residue number reindexed from 1) D146 A148 R150 N151 D164 S173 L185
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 T6E A A586 L608 F633 Y635 M636 F688 L699 I708 G709 D710 F711 A43 L65 F90 Y92 M93 F142 L153 I162 G163 D164 F165 MOAD: ic50=0.012uM
PDBbind-CN: -logKd/Ki=7.92,IC50=0.012uM
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:4at4, PDBe:4at4, PDBj:4at4
PDBsum4at4
PubMed22902478
UniProtQ16620|NTRK2_HUMAN BDNF/NT-3 growth factors receptor (Gene Name=NTRK2)

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