Structure of PDB 4ibm Chain B

Receptor sequence
>4ibmB (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
DEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESA
SLRERIEFLNEASVMKGFTCHHVVRLLGVVSPTLVVMELMAHGDLKSYLR
SLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCM
VAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTS
SDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYLDQPDNCPERVT
DLMRMCWQFNPNMRPTFLEIVNLLKDDLHPSFPEVSFFHSEENK
3D structure
PDB4ibm A highly selective dual insulin receptor (IR)/insulin-like growth factor 1 receptor (IGF-1R) inhibitor derived from an extracellular signal-regulated kinase (ERK) inhibitor.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1132 A1134 R1136 N1137 D1150 E1159 L1171
Catalytic site (residue number reindexed from 1) D143 A145 R147 N148 D161 E170 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 IR1 B L1002 A1028 M1076 E1077 M1079 A1080 G1082 M1139 D1150 M1153 L16 A42 M87 E88 M90 A91 G93 M150 D161 M164 MOAD: ic50=1.8uM
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:4ibm, PDBe:4ibm, PDBj:4ibm
PDBsum4ibm
PubMed23935097
UniProtP06213|INSR_HUMAN Insulin receptor (Gene Name=INSR)

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