Target Binding Site Detail

Content Navigation (  All   None )                                      
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 L-betagamma-meATP Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(CP(=O)(O)O)O)O)O)N
InChI 1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-31(24,25)28-30(22,23)4-29(19,20)21/h2-3,5,7-8,11,17-18H,1,4H2,(H,22,23)(H,24,25)(H2,12,13,14)(H2,19,20,21)/t5-,7-,8-,11-/m1/s1
InChIKey UFZTZBNSLXELAL-IOSLPCCCSA-N
PubChem Compound ID 91532
Drug Binding Sites of Target  Top
PDB ID: 4MNE      Crystal structure of the BRAF:MEK1 complex
Method X-ray diffraction Resolution 2.85 Å Mutation No [1]
PDB Sequence
DWEIPDGQIT
458
VGQRIGGTVY
472
KGKWHGDVAV
482
KMLNVTAPTP
492
QQLQAFKNEV
502

GVLRKTRHVN
512
ILLFMGYSTK
522
PQLAIVTQWC
532
EGSSLYHHLH
542
IIETKFEMIK
552

LIDIARQTAQ
562
GMDYLHAKSI
572
IHRDLKSNNI
582
FLHEDLTVKI
592
GDFGLATVKS
602

RWSGSHQFEQ
612
LSGSILWMAP
622
EVIRMQDKNP
632
YSFQSDVYAF
642
GIVLYELMTG
652

QLPYSNINNR
662
DQIIFMVGRG
672
YLSPDLSKVR
682
SNCPKAMKRL
692
MAECLKKKRD
702

ERPLFPQILA
712
SIELLARSLP
722
Residue
Distance (Å)
ARG662
4.959
Residue
Distance (Å)
PDB ID: 6U2G      BRAF-MEK complex with AMP-PCP bound to BRAF
Method X-ray diffraction Resolution 2.89 Å Mutation No [2]
PDB Sequence
EIPDGQITVG
460
QRIGSGSFGT
470
VYKGKWHGDV
480
AVKMLNVTAP
490
TPQQLQAFKN
500

EVGVLRKTRH
510
VNILLFMGYS
520
TKPQLAIVTQ
530
WCEGSSLYHH
540
LHIIETKFEM
550

IKLIDIARQT
560
AQGMDYLHAK
570
SIIHRDLKSN
580
NIFLHEDLTV
590
KIGDFGLATV
600

KSEQLSGSIL
618
WMAPEVIRMQ
628
DKNPYSFQSD
638
VYAFGIVLYE
648
LMTGQLPYSN
658

INNRDQIIFM
668
VGRGYLSPDL
678
SKVRSNCPKA
688
MKRLMAECLK
698
KKRDERPLFP
708

QILASIELLA
718
RSLP
Residue
Distance (Å)
ILE463
3.394
GLY464
3.422
SER465
3.876
GLY466
3.159
SER467
2.774
PHE468
3.793
GLY469
3.582
VAL471
2.809
ALA481
3.671
LYS483
3.613
LEU514
3.936
THR529
3.981
Residue
Distance (Å)
GLN530
2.868
TRP531
3.385
CYS532
3.349
SER536
4.614
HIS539
4.456
ASP576
2.515
LYS578
3.107
ASN580
3.413
ASN581
2.749
PHE583
3.527
ASP594
2.994
References  Top
REF 1 Structure of the BRAF-MEK complex reveals a kinase activity independent role for BRAF in MAPK signaling. Cancer Cell. 2014 Sep 8;26(3):402-413.
REF 2 Negative regulation of RAF kinase activity by ATP is overcome by 14-3-3-induced dimerization. Nat Struct Mol Biol. 2020 Feb;27(2):134-141.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.