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6V34

Crystal structure of BRAF V600E oncogenic mutant in complex with TAK-580

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue QOP A 801
ChainResidue
AALA481
ACYS532
AHIS574
AILE592
AGLY593
AASP594
ALYS483
AGLU501
ALEU505
ALEU514
AILE527
ATHR529
AGLN530
ATRP531

site_idAC2
Number of Residues17
Detailsbinding site for residue QOP B 801
ChainResidue
BVAL471
BALA481
BLYS483
BGLU501
BVAL504
BLEU505
BLEU514
BILE527
BTHR529
BGLN530
BTRP531
BCYS532
BLEU567
BHIS574
BILE592
BGLY593
BASP594

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
AILE463-LYS483

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
AILE572-LEU584

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP576
BASP576

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE463
ALYS483
BILE463
BLYS483

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
AARG671
BARG671

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581
ChainResidueDetails
ALYS578
BLYS578

227344

PDB entries from 2024-11-13

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