Structure of PDB 4r5y Chain A

Receptor sequence
>4r5yA (length=253) Species: 9606 (Homo sapiens) [Search protein sequence]
DWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAF
KNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHASETKF
EMKKLIDIARQTARGMDYLHAKSIIHRDLKSNNIFLHEDNTVKIGDFGSI
LWMAPEVIRMQDSNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIE
MVGRGSLSPDLSKVRSNCPKRMKRLMAECLKKKRDERPSFPRILAEIEEL
ARE
3D structure
PDB4r5y BGB-283, a Novel RAF Kinase and EGFR Inhibitor, Displays Potent Antitumor Activity in BRAF-Mutated Colorectal Cancers.
ChainA
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D576 K578 N580 N581 D594 S616
Catalytic site (residue number reindexed from 1) D128 K130 N132 N133 D146 S149
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 3K3 A V471 A481 K483 E501 L505 I527 T529 W531 C532 F583 D594 V23 A33 K35 E53 L57 I79 T81 W83 C84 F135 D146 PDBbind-CN: -logKd/Ki=7.64,IC50=23nM
BindingDB: IC50=23nM
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
View graph for
Biological Process
External links
PDB RCSB:4r5y, PDBe:4r5y, PDBj:4r5y
PDBsum4r5y
PubMed26208524
UniProtP15056|BRAF_HUMAN Serine/threonine-protein kinase B-raf (Gene Name=BRAF)

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