Structure of PDB 4at3 Chain A

Receptor sequence
>4at3A (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
GAMDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCKILVAVKTLASD
NARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFL
RAHGPDAVLMANPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRN
CLVGENLLVKIGDFGMSRYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTE
SDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVY
ELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG
3D structure
PDB4at3 The Crystal Structures of Trka and Trkb Suggest Key Regions for Achieving Selective Inhibition.
ChainA
Resolution1.77 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) D145 A147 R149 N150 D163 S170 L182
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 LTI A L560 F565 A586 F633 Y635 M636 G639 N697 L699 G709 L21 F26 A43 F88 Y90 M91 G94 N150 L152 G162 MOAD: ic50=0.004uM
PDBbind-CN: -logKd/Ki=8.40,IC50=0.004uM
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:4at3, PDBe:4at3, PDBj:4at3
PDBsum4at3
PubMed22902478
UniProtQ16620|NTRK2_HUMAN BDNF/NT-3 growth factors receptor (Gene Name=NTRK2)

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