Structure of PDB 3rhk Chain B

Receptor sequence
>3rhkB (length=299) Species: 9606 (Homo sapiens) [Search protein sequence]
LLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHG
TLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGI
CLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYL
ASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKL
PVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVY
LLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTF
3D structure
PDB3rhk Discovery of a novel mode of protein kinase inhibition characterized by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197.
ChainB
Resolution1.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1204 A1206 R1208 N1209 D1222 A1243
Catalytic site (residue number reindexed from 1) D159 A161 R163 N164 D177 A198
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 M97 B I1084 G1085 F1089 V1092 A1108 K1110 Y1159 M1160 G1163 M1211 F1223 I39 G40 F44 V47 A63 K65 Y114 M115 G118 M166 F178 MOAD: ic50=520nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3rhk, PDBe:3rhk, PDBj:3rhk
PDBsum3rhk
PubMed21454604
UniProtP08581|MET_HUMAN Hepatocyte growth factor receptor (Gene Name=MET)

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