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3II5

The Complex of wild-type B-RAF with Pyrazolo pyrimidine inhibitor

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 Residues11
DetailsBINDING SITE FOR RESIDUE 831 A 1
ChainResidue
AHOH16
APHE594
BARG670
AILE462
ALYS482
AGLU500
ALEU513
ATHR528
AHIS573
AGLY592
AASP593

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 726
ChainResidue
AHOH6
AASP447
ATRP449
AARG505
BTRP449
BARG505

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 2
ChainResidue
AGLN529
ATHR588
ALYS590
BLYS590

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 831 B 1
ChainResidue
BLYS482
BGLU500
BLEU504
BILE526
BTHR528
BILE591
BGLY592
BASP593
BPHE594

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
AILE462-LYS482

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
AILE571-LEU583

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
AASP575
BASP575

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE462
ALYS482
BILE462
BLYS482

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Breakpoint for translocation to form KIAA1549-BRAF fusion protein
ChainResidueDetails
AMET437
BMET437

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER445
BSER445

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER446
BSER446

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
AARG670
BARG670

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581
ChainResidueDetails
ALYS577
BLYS577

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP575
AASN579

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP575
BASN579

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP575
ALYS577

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP575
BLYS577

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ASER615
AASP575
ALYS577

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BSER615
BASP575
BLYS577

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN580
AASP575
ALYS577

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN580
BASP575
BLYS577

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PDB entries from 2024-07-10

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