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2FB8

Structure of the B-Raf kinase domain bound to SB-590885

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 Residues12
DetailsBINDING SITE FOR RESIDUE 215 B 101
ChainResidue
ATYR673
BPHE583
BASP594
BASN661
BALA481
BLYS483
BGLU501
BTHR529
BTRP531
BCYS532
BTYR538
BILE543

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 215 A 102
ChainResidue
AILE463
AGLY464
AVAL471
AALA481
ALYS483
AGLU501
ATHR529
ACYS532
APHE583
AASP594

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: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER446
BSER446

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER447
BSER447

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
AARG671
BARG671

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:23907581
ChainResidueDetails
ALYS578
BLYS578

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN580
AASP576

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN580
BASP576

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS578
AASP576

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS578
BASP576

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS578
AASP576
ASER616

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS578
BASP576
BSER616

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS578
AASP576
AASN581

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS578
BASP576
BASN581

223166

PDB entries from 2024-07-31

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