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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2B5U

Crystal Structure Of Colicin E3 V206C Mutant In Complex With Its Immunity Protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005727cellular_componentextrachromosomal circular DNA
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0016829molecular_functionlyase activity
A0019843molecular_functionrRNA binding
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0043022molecular_functionribosome binding
A0044325molecular_functiontransmembrane transporter binding
B0005515molecular_functionprotein binding
B0015643molecular_functiontoxic substance binding
B0030153biological_processbacteriocin immunity
C0000049molecular_functiontRNA binding
C0003723molecular_functionRNA binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005727cellular_componentextrachromosomal circular DNA
C0016787molecular_functionhydrolase activity
C0016788molecular_functionhydrolase activity, acting on ester bonds
C0016829molecular_functionlyase activity
C0019843molecular_functionrRNA binding
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0043022molecular_functionribosome binding
C0044325molecular_functiontransmembrane transporter binding
D0005515molecular_functionprotein binding
D0015643molecular_functiontoxic substance binding
D0030153biological_processbacteriocin immunity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIT C 601
ChainResidue
CARG495
CTYR519
CLYS544
CARG545
CASN546
CHOH670
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIT A 602
ChainResidue
AASN546
ATYR550
AHOH699
AARG495
ATYR519
AARG545
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues372
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues268
DetailsRegion: {"description":"Receptor-binding (R) domain","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues10
DetailsRegion: {"description":"Linker","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues192
DetailsRegion: {"description":"Ribosome inactivating activity"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues188
DetailsRegion: {"description":"Cytotoxic RNase (C) domain","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues42
DetailsRegion: {"description":"Binding of immunity protein"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues252
DetailsCoiled coil: {"evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14528295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JCH","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1UJW","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues12
DetailsMotif: {"description":"Hairpin","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14528295","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues132
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11741540","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsSite: {"description":"Stabilizes positive charge on His-513","evidences":[{"source":"PubMed","id":"20852642","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1jch
ChainResidueDetails
AASP510
AHIS513
AARG545
AGLU517
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1jch
ChainResidueDetails
CASP510
CHIS513
CARG545
CGLU517
site_idMCSA1
Number of Residues4
DetailsM-CSA 530
ChainResidueDetails
AASP510electrostatic stabiliser, increase acidity
AHIS513promote heterolysis, proton acceptor, proton donor
AGLU517increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AARG545electrostatic stabiliser
site_idMCSA2
Number of Residues4
DetailsM-CSA 530
ChainResidueDetails
CASP510electrostatic stabiliser, increase acidity
CHIS513promote heterolysis, proton acceptor, proton donor
CGLU517increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
CARG545electrostatic stabiliser

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PDB entries from 2025-11-05

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