Structure of PDB 3o23 Chain A

Receptor sequence
>3o23A (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
EWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAAS
MRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSY
LRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARN
CMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFT
TYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDM
LFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSE
3D structure
PDB3o23 Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: Advantages in comparison with competitive inhibitors
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1135 R1139 N1140 D1153 E1162
Catalytic site (residue number reindexed from 1) D145 R149 N150 D163 E172
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 MQY A K1033 M1054 V1062 M1079 M1082 F1131 M1142 D1153 M1156 K43 M64 V72 M89 M92 F141 M152 D163 M166 MOAD: ic50=0.5uM
PDBbind-CN: -logKd/Ki=6.30,IC50=0.5uM
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:3o23, PDBe:3o23, PDBj:3o23
PDBsum3o23
PubMed21441024
UniProtP08069|IGF1R_HUMAN Insulin-like growth factor 1 receptor (Gene Name=IGF1R)

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