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 1k82 Chain C Binding Site BS03

Receptor Information >1k82 Chain C (length=260) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] PELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLS VQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGK VLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKK TAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARV IKAVLLRSIEQGGTTLKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQR ATFYCRQCQK

Ligand information >1k82 Chain L (length=13) [Search DNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure] ccaggacgaagcc

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 1k82 Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA. Resolution 2.1 Å Binding residue (original residue number in PDB) K149 K150 T151 Binding residue (residue number reindexed from 1) K149 K150 T151

Enzymatic activity Catalytic site (original residue number in PDB) P1 E2 Catalytic site (residue number reindexed from 1) P1 E2 Enzyme Commision number 3.2.2.23: DNA-formamidopyrimidine glycosylase. 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.

Gene Ontology Molecular Function GO:0000703 oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity GO:0003676 nucleic acid binding GO:0003677 DNA binding GO:0003684 damaged DNA binding GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity GO:0004519 endonuclease activity GO:0008270 zinc ion binding GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity GO:0016787 hydrolase activity GO:0016798 hydrolase activity, acting on glycosyl bonds GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds GO:0016829 lyase activity GO:0019104 DNA N-glycosylase activity GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity GO:0046872 metal ion binding GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity

	Biological Process
GO:0006281	DNA repair
GO:0006284	base-excision repair
GO:0006974	DNA damage response

	Cellular Component
GO:0005737	cytoplasm

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component