Structure of PDB 5dg5 Chain A

Receptor sequence
>5dg5A (length=297) Species: 9606 (Homo sapiens) [Search protein sequence]
TVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLD
NDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRS
EGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKK
FVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKW
MALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQG
RRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
3D structure
PDB5dg5 Altiratinib Inhibits Tumor Growth, Invasion, Angiogenesis, and Microenvironment-Mediated Drug Resistance via Balanced Inhibition of MET, TIE2, and VEGFR2.
ChainA
Resolution2.6 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) D155 A157 R159 N160 D173 A194
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 5B4 A V1092 A1108 K1110 M1131 L1140 L1157 Y1159 M1160 G1163 L1195 F1200 M1211 A1221 D1222 F1223 V43 A59 K61 M82 L91 L108 Y110 M111 G114 L146 F151 M162 A172 D173 F174
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:5dg5, PDBe:5dg5, PDBj:5dg5
PDBsum5dg5
PubMed26285778
UniProtP08581|MET_HUMAN Hepatocyte growth factor receptor (Gene Name=MET)

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