Structure of PDB 4agc Chain A

Receptor sequence
>4agcA (length=304) Species: 9606 (Homo sapiens) [Search protein sequence]
YLSIVMDPDELPLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGID
KTATCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTK
PGGPLMVIVEFCKFGNLSTYLRSKRNEFVPYYKDFLTLEHLICYSFQVAK
GMEFLASRKCIHRDLAARNILLSEKNVVKICDFGLARDIYKDPDYVRKGD
ARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKIDEE
FCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNLL
QANA
3D structure
PDB4agc Molecular Conformations, Interactions, and Properties Associated with Drug Efficiency and Clinical Performance Among Vegfr Tk Inhibitors.
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) D1028 A1030 R1032 N1033 D1046 D1064
Catalytic site (residue number reindexed from 1) D164 A166 R168 N169 D182 D200
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 AXI A V848 A866 K868 E885 V914 V916 E917 F918 C919 K920 G922 L1035 C1045 D1046 F1047 A1168 V41 A59 K61 E78 V107 V109 E110 F111 C112 K113 G115 L171 C181 D182 F183 A304 MOAD: Ki=0.02nM
PDBbind-CN: -logKd/Ki=10.70,Ki=0.020nM
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
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Biological Process
External links
PDB RCSB:4agc, PDBe:4agc, PDBj:4agc
PDBsum4agc
PubMed22988103
UniProtP35968|VGFR2_HUMAN Vascular endothelial growth factor receptor 2 (Gene Name=KDR)

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