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

Structure of PDB 6qya Chain D

Receptor sequence >6qyaD (length=315) Species: 1351 (Enterococcus faecalis) [Search protein sequence] MEEAYLALGKKILEEGHFKEDRTGTGTYSLFGYQMRFDLAKGFPLLTTKR VPFGLIKSELLWFLKGDTNIRYLLERNNHIWDEWAFERYVKSADYQGPDM TDFGHRVLQDPAFAEQYKEEHQKFCDAILNDAEFAEKYGELGNIYGAQWR HWETKDGSFIDQLANVIEMIKTNPDSRRLIVSAWNPEDVPSMALPPCHTM FQFYVNEGKLSCQLYQRSADVFLGVPFNIASYALLTHLIAHETGLEVGEF VHTLGDAHLYQNHVEQMQEQLSREVRSFPTLVLNPDKASVFDFDMEDIKV EGYDPHPTIKAPIAV

3D structure PDB 6qya Structural Comparison ofEnterococcus faecalisand Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities. Chain D Resolution 1.76 Å 3D structure Catalytic site residues are labeled in the 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 Catalytic site (original residue number in PDB) E59 W81 Y145 C197 R217 D220 Catalytic site (residue number reindexed from 1) E59 W81 Y145 C197 R217 D220 Enzyme Commision number 2.1.1.45: thymidylate synthase.

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 UMP D R177 R178 R177 R178 BS02 FFO D L55 W81 W84 L194 C197 D220 L223 I313 L55 W81 W84 L194 C197 D220 L223 I313

Gene Ontology Molecular Function GO:0004799 thymidylate synthase activity GO:0008168 methyltransferase activity GO:0016741 transferase activity, transferring one-carbon groups

	Biological Process
GO:0006231	dTMP biosynthetic process
GO:0006235	dTTP biosynthetic process
GO:0009165	nucleotide biosynthetic process
GO:0032259	methylation

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component