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1JCH

Crystal Structure of Colicin E3 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
A0032413biological_processnegative regulation of ion transmembrane transporter activity
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
C0032413biological_processnegative regulation of ion transmembrane transporter activity
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 Residues5
DetailsBINDING SITE FOR RESIDUE CIT A 601
ChainResidue
AARG545
AASN546
AILE547
ALYS549
AHOH925

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CIT A 602
ChainResidue
AHOH5980
AGLN512
AHIS513
AHOH922
AHOH983

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CIT C 5601
ChainResidue
CARG545
CASN546
CILE547
CLYS549
CHOH917
CHOH5925

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CIT C 5602
ChainResidue
CGLN512
CHIS513
CHOH980
CHOH5922
CHOH5983

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 701
ChainResidue
APHE378
CVAL139
CLEU140
CASP187

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 702
ChainResidue
ALYS458
BGLY1
BASP27
BTYR79
BASP81
BGLY82

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 5701
ChainResidue
AVAL139
ALEU140
AASP187
CPHE378

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 5702
ChainResidue
CLYS458
DGLY1
DASP27
DTYR79
DASP81
DGLY82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
ChainResidueDetails
AHIS513
CHIS513

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
ChainResidueDetails
AGLU517
CGLU517

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:11741540
ChainResidueDetails
AARG545
CARG545

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642
ChainResidueDetails
AASP510
CASP510

Catalytic Information from CSA
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

218853

PDB entries from 2024-04-24

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