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7BTQ

EcoR124I-DNA in the Restriction-Alleviation State

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0009007molecular_functionsite-specific DNA-methyltransferase (adenine-specific) activity
A0009307biological_processDNA restriction-modification system
A0016740molecular_functiontransferase activity
A0032259biological_processmethylation
D0003676molecular_functionnucleic acid binding
D0003677molecular_functionDNA binding
D0008168molecular_functionmethyltransferase activity
D0008170molecular_functionN-methyltransferase activity
D0009007molecular_functionsite-specific DNA-methyltransferase (adenine-specific) activity
D0009307biological_processDNA restriction-modification system
D0016740molecular_functiontransferase activity
D0032259biological_processmethylation
E0003677molecular_functionDNA binding
E0009307biological_processDNA restriction-modification system
F0000166molecular_functionnucleotide binding
F0003677molecular_functionDNA binding
F0004518molecular_functionnuclease activity
F0004519molecular_functionendonuclease activity
F0005524molecular_functionATP binding
F0006304biological_processDNA modification
F0009035molecular_functiontype I site-specific deoxyribonuclease activity
F0009307biological_processDNA restriction-modification system
F0016787molecular_functionhydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00092
Number of Residues7
DetailsN6_MTASE N-6 Adenine-specific DNA methylases signature. IVSNPPY
ChainResidueDetails
AILE299-TYR305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues550
DetailsRegion: {"description":"Catalytic domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues58
DetailsRegion: {"description":"C-terminal tail","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q89Z59","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues45
DetailsRegion: {"description":"Conserved region 1","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues149
DetailsRegion: {"description":"Target-recognition domain 2","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues145
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues219
DetailsRegion: {"description":"Motor 1 domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues232
DetailsRegion: {"description":"Motor 2 domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsRegion: {"description":"Motor 2-helicase linker","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues128
DetailsRegion: {"description":"Helicase domain","evidences":[{"source":"PubMed","id":"32483229","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsMotif: {"description":"DEAH box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250059

PDB entries from 2026-03-04

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