Structure of PDB 4at5 Chain A

Receptor sequence
>4at5A (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
GAMDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLKILVAVKTLKDAS
DNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKF
LRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLA
TRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYR
KFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC
PQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG
3D structure
PDB4at5 The Crystal Structures of Trka and Trkb Suggest Key Regions for Achieving Selective Inhibition.
ChainA
Resolution1.71 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) D148 A150 R152 N153 D166 S175 L187
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 MUJ A A586 L608 V617 F633 Y635 M636 F688 N697 L699 G709 D710 F711 A42 L64 V73 F89 Y91 M92 F144 N153 L155 G165 D166 F167 MOAD: ic50=0.038uM
PDBbind-CN: -logKd/Ki=7.42,IC50=0.038uM
BindingDB: Kd=36nM
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:4at5, PDBe:4at5, PDBj:4at5
PDBsum4at5
PubMed22902478
UniProtQ16620|NTRK2_HUMAN BDNF/NT-3 growth factors receptor (Gene Name=NTRK2)

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