Structure of PDB 4xlv Chain A Binding Site BS02
Receptor Information
>4xlv Chain A (length=310) Species:
9606
(Homo sapiens) [
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SASDVFPSSVYVPDEWEVSREKITLLRELGQGSFGMVYEGNARDIIKGEA
ETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTL
VVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYL
NAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPV
RWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVM
DGGYLDQPDNCPERVTDLMRMCWQFNPNMRPTFLEIVNLLKDDLHPSFPE
VSFFHSEENK
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
4xlv Chain A Residue 1302 [
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Receptor-Ligand Complex Structure
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PDB
4xlv
The insulin and IGF1 receptor kinase domains are functional dimers in the activated state.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
N1137 D1150
Binding residue
(residue number reindexed from 1)
N164 D177
Annotation score
1
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.
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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Cellular Component
External links
PDB
RCSB:4xlv
,
PDBe:4xlv
,
PDBj:4xlv
PDBsum
4xlv
PubMed
25758790
UniProt
P06213
|INSR_HUMAN Insulin receptor (Gene Name=INSR)
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