Structure of PDB 6xfp Chain A

Receptor sequence
>6xfpA (length=272) Species: 9606 (Homo sapiens) [Search protein sequence]
DWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAF
KNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYKHLHASETKF
EMKKLIDIARQTARGMDYLHAKSIIHRDLKSNNIFLHEDNTVKIGDFGLA
TVKSRWSGSHQFEQLSGSILWMAPEVIRMQDSNPYSFQSDVYAFGIVLYE
LMTGQLPYSNINNRDQIIEMVGRGSLSPDLSKVRSNCPKRMKRLMAECLK
KKRDERPSFPRILAEIEELARE
3D structure
PDB6xfp ARAF mutations confer resistance to the RAF inhibitor belvarafenib in melanoma.
ChainA
Resolution2.0 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) D576 K578 N580 N581 D594 S616
Catalytic site (residue number reindexed from 1) D128 K130 N132 N133 D146 S168
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 V1Y A A481 K483 E501 L505 L514 I527 T529 W531 C532 G593 D594 F595 A33 K35 E53 L57 L66 I79 T81 W83 C84 G145 D146 F147 BindingDB: IC50=56nM
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:6xfp, PDBe:6xfp, PDBj:6xfp
PDBsum6xfp
PubMed33953400
UniProtP15056|BRAF_HUMAN Serine/threonine-protein kinase B-raf (Gene Name=BRAF)

[Back to BioLiP]