Structure of PDB 3pp0 Chain A

Receptor sequence
>3pp0A (length=286) Species: 9606 (Homo sapiens) [Search protein sequence]
APNQALLRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVL
RENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGC
LLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKS
PNHVKITDFGLARLLDIDETEYHAGKVPIKWMALESILRRRFTHQSDVWS
YGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVK
CWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNED
3D structure
PDB3pp0 Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D845 A847 R849 N850 D863
Catalytic site (residue number reindexed from 1) D140 A142 R144 N145 D158
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 03Q A L726 V734 A751 K753 E770 M774 L785 L796 T798 L800 M801 R849 L852 T862 D863 F864 L21 V29 A46 K48 E65 M69 L80 L91 T93 L95 M96 R144 L147 T157 D158 F159 MOAD: ic50=11nM
PDBbind-CN: -logKd/Ki=7.96,IC50=11nM
BindingDB: IC50=11nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3pp0, PDBe:3pp0, PDBj:3pp0
PDBsum3pp0
PubMed21454582
UniProtP04626|ERBB2_HUMAN Receptor tyrosine-protein kinase erbB-2 (Gene Name=ERBB2)

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