Structure of PDB 5c9c Chain B

Receptor sequence
>5c9cB (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
DWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAF
KNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKF
EMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLS
ILWMAPEVIRMNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMV
GRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLAR
S
3D structure
PDB5c9c Inhibition of RAF Isoforms and Active Dimers by LY3009120 Leads to Anti-tumor Activities in RAS or BRAF Mutant Cancers.
ChainB
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D575 K577 N579 N580 D593 S615
Catalytic site (residue number reindexed from 1) D128 K130 N132 N133 D146 S150
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 4Z5 B A480 K482 E500 L504 L513 I526 T528 W530 C531 G592 D593 F594 A33 K35 E53 L57 L66 I79 T81 W83 C84 G145 D146 F147 BindingDB: IC50=31nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5c9c, PDBe:5c9c, PDBj:5c9c
PDBsum5c9c
PubMed26343583
UniProtP15056|BRAF_HUMAN Serine/threonine-protein kinase B-raf (Gene Name=BRAF)

[Back to BioLiP]