Structure of PDB 4pmm Chain A

Receptor sequence
>4pmmA (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
CVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLDKMLVAVKALKESARQD
FQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGP
DAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNC
LVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTT
ESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEV
YAIMRGCWQREPQQRHSIKDVHARLQALAQAHHHH
3D structure
PDB4pmm Maximizing diversity from a kinase screen: identification of novel and selective pan-Trk inhibitors for chronic pain.
ChainA
Resolution2.0 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) D144 A146 R148 N149 D162 S171 L183
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 31V A A542 K544 E560 F589 Y591 M592 L657 G667 D668 F669 A39 K41 E54 F83 Y85 M86 L151 G161 D162 F163 MOAD: Kd=27nM
PDBbind-CN: -logKd/Ki=7.57,Kd=27nM
BindingDB: IC50=662nM,Kd=27nM
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:4pmm, PDBe:4pmm, PDBj:4pmm
PDBsum4pmm
PubMed24914455
UniProtP04629|NTRK1_HUMAN High affinity nerve growth factor receptor (Gene Name=NTRK1)

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