Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4FXH

Crystal structure of the isolated E. coli RelE toxin, P212121 form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000976molecular_functiontranscription cis-regulatory region binding
A0001217molecular_functionDNA-binding transcription repressor activity
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0005515molecular_functionprotein binding
A0006355biological_processregulation of DNA-templated transcription
A0006402biological_processmRNA catabolic process
A0016787molecular_functionhydrolase activity
A0017148biological_processnegative regulation of translation
A0019843molecular_functionrRNA binding
A0032993cellular_componentprotein-DNA complex
A0034198biological_processcellular response to amino acid starvation
A0040008biological_processregulation of growth
A0043022molecular_functionribosome binding
A0044010biological_processsingle-species biofilm formation
A0045892biological_processnegative regulation of DNA-templated transcription
A0046677biological_processresponse to antibiotic
A0097351molecular_functiontoxin sequestering activity
A0110001cellular_componenttoxin-antitoxin complex
B0000976molecular_functiontranscription cis-regulatory region binding
B0001217molecular_functionDNA-binding transcription repressor activity
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
B0005515molecular_functionprotein binding
B0006355biological_processregulation of DNA-templated transcription
B0006402biological_processmRNA catabolic process
B0016787molecular_functionhydrolase activity
B0017148biological_processnegative regulation of translation
B0019843molecular_functionrRNA binding
B0032993cellular_componentprotein-DNA complex
B0034198biological_processcellular response to amino acid starvation
B0040008biological_processregulation of growth
B0043022molecular_functionribosome binding
B0044010biological_processsingle-species biofilm formation
B0045892biological_processnegative regulation of DNA-templated transcription
B0046677biological_processresponse to antibiotic
B0097351molecular_functiontoxin sequestering activity
B0110001cellular_componenttoxin-antitoxin complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 101
ChainResidue
ALYS17
BLYS29
BLYS54
BLEU55
BARG56
BHOH222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"24251350","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"24251350","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"24251350","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239149

건을2025-07-23부터공개중

PDB statisticsPDBj update infoContact PDBjnumon