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5ITA

Crystal Structure of BRAF Kinase Domain Bound to AZ-VEM

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 Residues15
Detailsbinding site for residue 6DC A 801
ChainResidue
AILE463
APHE583
AGLY593
AASP594
APHE595
AGLY596
AHOH949
AALA481
ALYS483
ALEU514
ATHR529
AGLN530
ATRP531
ACYS532
AASN581

site_idAC2
Number of Residues14
Detailsbinding site for residue 6DC B 801
ChainResidue
BILE463
BALA481
BLYS483
BLEU505
BLEU514
BTHR529
BGLN530
BTRP531
BCYS532
BPHE583
BGLY593
BASP594
BPHE595
BHOH928

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
BILE463
BLYS483
AILE463
ALYS483

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
BLYS578
ALYS578

219869

PDB entries from 2024-05-15

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