Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 8cav Chain B

Receptor sequence
>8cavB (length=858) Species: 2020 (Thermomonospora curvata) [Search protein sequence]
ATPTEQELRAELTGPVTGAGRQIHARGVWLAVDDPAFHLPRQGWKIHLSA
RPATLQETIRRMLPAVLAVPCHFKVVRSGRHLQDLNSANNHPGSIGKAVT
IYPSPEDVAPLARRLAEDLAGMAGPRICSDRRVRPDAPVYYRYGPFHPCY
DINDDGDLELVVTDPQGNTHPGAADDSFWQPHWSPDPLTGATPHPAPSDG
PAAPVLLGGRYRVVRGLTRNGKGCVYRAIDTTDNRPVIIKEARAHVNEDT
LGRDSRLRLRNERYVLHLLRDLDDVPKVIDHFRHEDREYLAITDLGALAL
GQDVAENGLYVADPAPPGRSLRALATALLELLDHVHRRGVLVRDLTPTNV
VLDDATGRPRLVDFEISHAEDPQLYGWTPGYSPPEQERDEPATVEADYYS
LGATLFYAATGLPPTWMTGDPGNHDPRRAAEVLAGRGGMSGTILGLLDPD
PARRRAAADDIRAGRFTDAPPPPPPSARQRARRLAAAIAHSLTELSRHAA
DLMSGKDFTGGLVGSPINLYRGAAGMGMELLRHDEPSRALARGLAYWTGG
FRALRNGRPGLYTGDTGIAVFIAEAGATLGDETLLKIAEPLARPVLSRIT
ATDQHTGLAGIGTGQLLLWRLTKDAGRLELADACARRLLARDLTAELQEN
PPDYADCGAVSRTLGFAHGLAGIVHFLRDHHAATGETATEAALHKGCDTL
LEHLPPLLEAARAVSAKPMHASFCQGLAGIGAALARTGRDLGADDHLQAA
REAAAACLELAPRMYALTQCCGLAGIGELFLDLCQITGDRTYAQWADRIA
DLILARAGGSPEAPVFPDTSLHGSSGGWSIGTSGVVSFLRRLGDPAAPRL
WLDPPAGT
3D structure
PDB8cav Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL.
ChainB
Resolution2.87 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide B G213 R265 H286 F287 R288 H289 G208 R260 H281 F282 R283 H284
BS02 ANP B V230 I243 K245 T298 D299 L300 T353 V367 D368 E370 V225 I238 K240 T293 D294 L295 T348 V362 D363 E365
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006468 protein phosphorylation
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0031179 peptide modification

View graph for
Molecular Function
View graph for
Biological Process
External links

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417