Structure of PDB 3hng Chain A

Receptor sequence
>3hngA (length=288) Species: 9606 (Homo sapiens) [Search protein sequence]
EVPLDEQCERPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSP
TCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGG
PLMVIVEYCKYGNLSNYLKSKRKEPITMEDLISYSFQVARGMEFLSSRKC
IHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKTRLPLKWMAPES
IFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMR
APEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLL
3D structure
PDB3hng Crystal structure of VEGFR1 in complex with N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamide
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1022 A1024 R1026 N1027 D1040
Catalytic site (residue number reindexed from 1) D154 A156 R158 N159 D172
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 8ST A K861 E878 V909 Y911 C912 L1029 C1039 D1040 F1041 K58 E75 V106 Y108 C109 L161 C171 D172 F173 PDBbind-CN: -logKd/Ki=6.74,IC50=0.18uM
BindingDB: IC50=180nM
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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3hng, PDBe:3hng, PDBj:3hng
PDBsum3hng
PubMed
UniProtP17948|VGFR1_HUMAN Vascular endothelial growth factor receptor 1 (Gene Name=FLT1)

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