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 4zcf Chain A Binding Site BS02

Receptor Information
>4zcf Chain A (length=616) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANSKQLAVLKANFPQCFDKNGAFIQEKLLEIIRASEKESYSLNWLGKSYA
RLLANLPPKTLLAEDKTHNQQEENKNSQHLLIKGDNLEVLKHMVNAYAEK
VKMIYIDPPYNTGKDGFVYNDDRFTPEQLSELAGIDLDEAKRILEFTTKG
SSSHSAWLTFIYPRLYIARELMREDGTIFISIDHNEFSQLKLVCDEIFGE
QNHVGDLVWKNATDNNPSNIAVEHEYIIVYTKNKEQLISEWKSNISDVKN
LLVNIGEEFASKYTGNELQEKYTQWFREHRSELWPLDRYKYIDKDGIYTG
SQSVHNPGKEGYRYDIIHPKTKKPCKQPLMGYRFPLDTMDRLLSEEKIIF
GDDENKIIELKVYAKDYKQKLSSVIHLDGRVATNELKELFPMTQPFNAKT
IKLVEDLISFACDGEGIVLDFFAGSGTTAHTVFNLNNKNKTSYQFITVQL
DEPTKKSDAMKHGYNTIFDLTKERLIRASKKNRDQGFKVYQLMPDFRAKD
ESELTFFDDVVLTPEQYDTLLTTWCLYDGSLLTTPIEDVDLGGYKAHLCD
GRLYLIAPNFTSEALKALLQKVDSDKDFAPNKVVFYGSNFSAKQMELNEA
LKSYANSIELDLVVRN
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure 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]
PDB4zcf Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I.
Resolution2.6 Å
Binding residue
(original residue number in PDB)
W301 R305 Y306 S320 N323 P324 Y329 R350 F351 P352 T355
Binding residue
(residue number reindexed from 1)
W284 R288 Y289 S303 N306 P307 Y312 R333 F334 P335 T338
Enzymatic activity
Enzyme Commision number 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific).
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0008168 methyltransferase activity
GO:0008170 N-methyltransferase activity
GO:0009007 site-specific DNA-methyltransferase (adenine-specific) activity
Biological Process
GO:0009307 DNA restriction-modification system
GO:0032259 methylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:4zcf, PDBe:4zcf, PDBj:4zcf
PDBsum4zcf
PubMed26067164
UniProtP12364|T3MO_ECOLX Type III restriction-modification enzyme EcoP15I Mod subunit (Gene Name=mod)

[Back to BioLiP]

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