Structure of PDB 4zcf Chain B

Receptor sequence
>4zcfB (length=612) Species: 562 (Escherichia coli) [Search protein sequence]
KKETIFEVETANSKQLAVLKANFPQCFDNGAFIQEKLLEIIRASEVELSK
ESYSLNWLGKSYARLLANLPPKTLLAEDKTHNQQEENKNSQHLLIKGDNL
EVLKHMVNAYAEKVKMIYIDPPYNTGKDGFVYNDDRKFTPEQLSELAGID
LDEAKRILEFTTKGSSSHSAWLTFIYPRLYIARELMREDGTIFISIDHNE
FSQLKLVCDEIFGEQNHVGDLVWKNATDNNPSNIAVEHEYIIVYTKKEQL
ISEWKSNISDVKNLLVNIGEEFASKYTGNELQEKYTQWFREHRSELWPLD
RYKYIDKDGIYTGSQSVHNPGKEGYRYDIIHPKTKKPCKQPLMGYRFPLD
TMDRLLSEEKIIFGDDEKIIELKVYAKDYKQKLSSVIHLDGRVATNELKE
LFPEMTQPFTNAKTIKLVEDLISFACDGEGIVLDFFAGSGTTAHTVFNLN
NKNKTSYQFITVQLDEPTKDKSDAMKHGYNTIFDLTKERLIRASKKNRDQ
GFKVYQLMPDFVVLTPEQYDTLLTTWCLYDGSLLTTPIEDVDLGGYKAHL
CDGRLYLIAPNFTALKALLQKDKDFAPNKVVFYGSNSAKQMELNEALKSY
ANKKELDLVVRN
3D structure
PDB4zcf Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I.
ChainB
Resolution2.6 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 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific).
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 dna B D123 P124 Y126 D131 N233 R397 T400 N416 D120 P121 Y123 D128 N230 R392 T395 N411
BS02 dna B N232 N233 D395 R397 V398 N229 N230 D390 R392 V393
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]