Structure of PDB 4fc0 Chain B

Receptor sequence
>4fc0B (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
DDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQA
FKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETK
FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGL
ATVKSRWGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYS
NINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLF
PQILASIELLARS
3D structure
PDB4fc0 Design and synthesis of novel DFG-out RAF/vascular endothelial growth factor receptor 2 (VEGFR2) inhibitors: 3. Evaluation of 5-amino-linked thiazolo[5,4-d]pyrimidine and thiazolo[5,4-b]pyridine derivatives.
ChainB
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D575 K577 N579 N580 D593 W603 S615
Catalytic site (residue number reindexed from 1) D129 K131 N133 N134 D147 W157 S159
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 0T2 B A480 K482 E500 L504 I526 T528 W530 C531 G533 H573 G592 D593 F594 A597 A34 K36 E54 L58 I80 T82 W84 C85 G87 H127 G146 D147 F148 A151 BindingDB: IC50=69nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:4fc0, PDBe:4fc0, PDBj:4fc0
PDBsum4fc0
PubMed22883026
UniProtP15056|BRAF_HUMAN Serine/threonine-protein kinase B-raf (Gene Name=BRAF)

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