Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T99089 Target Info
Target Name Serine/threonine-protein kinase B-raf (BRAF)
Synonyms V-Raf murine sarcoma viral oncogene homolog B1; RAFB1; Proto-oncogene B-Raf; P94; BRAF1; BRAF(V599E); BRAF serine/threonine kinase; B-raf protein; B-Raf
Target Type Successful Target
Gene Name BRAF
Biochemical Class Kinase
UniProt ID
BRAF_HUMAN
Ligand General Information  Top
Ligand Name PLX-4720 Ligand Info
Canonical SMILES CCCS(=O)(=O)NC1=C(C(=C(C=C1)F)C(=O)C2=CNC3=C2C=C(C=N3)Cl)F
InChI 1S/C17H14ClF2N3O3S/c1-2-5-27(25,26)23-13-4-3-12(19)14(15(13)20)16(24)11-8-22-17-10(11)6-9(18)7-21-17/h3-4,6-8,23H,2,5H2,1H3,(H,21,22)
InChIKey YZDJQTHVDDOVHR-UHFFFAOYSA-N
PubChem Compound ID 24180719
Drug Binding Sites of Target  Top
PDB ID: 4WO5      Crystal structure of a BRAF kinase domain monomer
Method X-ray diffraction Resolution 2.83 Å Mutation Yes [1]
PDB Sequence
DDWEIPDGQI
457
TVGQRIGSGS
467
FGTVYKGKWH
477
GDVAVKMLNV
487
TAPTPQQLQA
497

FKNEVGVLRK
507
TRHVNILLFM
517
GYSTKPQLAI
527
VTQWCEGSSL
537
YHHLHASEKF
548

EMKKLIDIAR
558
QTARGMDYLH
568
AKSIIHRDLK
578
SNNIFLHEDN
588
TVKIGDFGLA
598

TVKSRWSFEQ
612
LSGSILWMAP
622
EVIRMNPYSF
635
QSDVYAFGIV
645
LYELMTGQLP
655

YSNINNRDQI
665
IEMVGRGSLS
675
PDLSKVRSNC
685
PKRMKRLMAE
695
CLKKKRDERP
705

SFPRILAEIE
715
ELAREL
Residue
Distance (Å)
ILE463
3.416
VAL471
3.319
ALA481
3.219
VAL482
3.686
LYS483
3.147
LEU505
3.572
LEU514
3.120
LEU515
4.552
PHE516
3.708
ILE527
3.882
THR529
2.947
Residue
Distance (Å)
GLN530
2.787
TRP531
3.339
CYS532
3.014
SER535
3.563
SER536
4.436
ASN581
4.697
PHE583
3.283
GLY593
3.399
ASP594
2.981
PHE595
3.007
GLY596
2.907
PDB ID: 3C4C      B-Raf Kinase in Complex with PLX4720
Method X-ray diffraction Resolution 2.57 Å Mutation Yes [2]
PDB Sequence
DDWEIPDGQI
457
TVGQRIGSGS
467
FGTVYKGKWH
477
GDVAVKMLNV
487
TAPTPQQLQA
497

FKNEVGVLRK
507
TRHVNILLFM
517
GYSTKPQLAI
527
VTQWCEGSSL
537
YHHLHASETK
547

FEMKKLIDIA
557
RQTARGMDYL
567
HAKSIIHRDL
577
KSNNIFLHED
587
NTVKIGDFGS
614

GSILWMAPEV
624
IRMQDSNPYS
634
FQSDVYAFGI
644
VLYELMTGQL
654
PYSNINNRDQ
664

IIEMVGRGSL
674
SPDLSKVRSN
684
CPKRMKRLMA
694
ECLKKKRDER
704
PSFPRILAEI
714

EELARELS
Residue
Distance (Å)
ILE463
3.658
VAL471
3.656
ALA481
3.371
VAL482
3.946
LYS483
3.414
LEU505
3.526
THR508
4.763
LEU514
3.425
LEU515
4.708
PHE516
3.867
Residue
Distance (Å)
ILE527
3.668
THR529
3.300
GLN530
3.007
TRP531
3.293
CYS532
2.959
PHE583
3.036
GLY593
4.280
ASP594
3.205
PHE595
2.488
GLY596
4.628
References  Top
REF 1 Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation. Nat Struct Mol Biol. 2015 Jan;22(1):37-43.
REF 2 Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity. Proc Natl Acad Sci U S A. 2008 Feb 26;105(8):3041-6.

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