Structure of PDB 3qti Chain A

Receptor sequence
>3qtiA (length=292) Species: 9606 (Homo sapiens) [Search protein sequence]
HIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDKI
HCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLV
VLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKFLASKKFVHRDL
AARNCMLDEKFTVKVADFGLARDMYDKEFLPVKWMALESLQTQKFTTKSD
VWSFGVLLWELMTRGAPPYPDFDITVYLLQGRRLLQPEYCPDPLYEVMLK
CWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVK
3D structure
PDB3qti A Drug Resistance Screen Using a Selective MET Inhibitor Reveals a Spectrum of Mutations That Partially Overlap with Activating Mutations Found in Cancer Patients.
ChainA
Resolution2.0 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
Catalytic site (residue number reindexed from 1) D149 A151 R153 N154 D167
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 3QT A I1084 A1108 Y1159 M1160 D1164 R1208 M1211 A1221 D1222 Y1230 I33 A53 Y104 M105 D109 R153 M156 A166 D167 Y175 MOAD: ic50=14nM
PDBbind-CN: -logKd/Ki=7.85,IC50=14nM
BindingDB: IC50=14nM
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:3qti, PDBe:3qti, PDBj:3qti
PDBsum3qti
PubMed21697284
UniProtP08581|MET_HUMAN Hepatocyte growth factor receptor (Gene Name=MET)

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