Structure of PDB 4xlv Chain A

Receptor sequence
>4xlvA (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
SASDVFPSSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEA
ETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTL
VVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYL
NAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPV
RWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVM
DGGYLDQPDNCPERVTDLMRMCWQFNPNMRPTFLEIVNLLKDDLHPSFPE
VSFFHSEENK
3D structure
PDB4xlv The insulin and IGF1 receptor kinase domains are functional dimers in the activated state.
ChainA
Resolution2.3 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) D159 A161 R163 N164 D177 E186 L198
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 ACP A L1002 V1010 A1028 K1030 M1076 M1079 D1083 M1139 D1150 L29 V37 A55 K57 M103 M106 D110 M166 D177
BS02 MG A N1137 D1150 N164 D177
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:4xlv, PDBe:4xlv, PDBj:4xlv
PDBsum4xlv
PubMed25758790
UniProtP06213|INSR_HUMAN Insulin receptor (Gene Name=INSR)

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