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8VYV

Cryo-EM Structure of the BRAF K601E monomer

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
CILE829-LYS849

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
CILE938-LEU950

site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFvrktfftlaf.CdfCrklLfqgfr.....CqtCgykfHqrCstevplm..C
ChainResidueDetails
CHIS235-CYS280

site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG41-VAL51

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR211-SER230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsZN_FING: Phorbol-ester/DAG-type => ECO:0000255|PROSITE-ProRule:PRU00226
ChainResidueDetails
CTHR234-CYS280
AARG127
BARG56
BARG127

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
CASP942
BMET1

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CHIS235
CCYS248
CCYS251
CCYS261
CCYS264
CHIS269
CCYS272
CCYS280

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
CILE829
CLYS849

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Breakpoint for translocation to form KIAA1549-BRAF fusion protein
ChainResidueDetails
CASP746
CMET804

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.8
ChainResidueDetails
CALA2
BSER207

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
CSER151
BSER210

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P28028
ChainResidueDetails
CSER333
CSER1158

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:11410590, ECO:0000269|Ref.8, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSEP365

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1508179
ChainResidueDetails
CTHR739

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|Ref.8
ChainResidueDetails
CTHR762

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.8
ChainResidueDetails
CSER765

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|Ref.8, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR767

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER812

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
CSER813

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
CARG1037

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.8, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSEP1137

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK1 => ECO:0000269|PubMed:19710016
ChainResidueDetails
CTHR1161

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581
ChainResidueDetails
CLYS944

237423

PDB entries from 2025-06-11

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