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1E44

ribonuclease domain of colicin E3 in complex with its immunity protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0015643molecular_functiontoxic substance binding
A0030153biological_processbacteriocin immunity
B0003723molecular_functionRNA binding
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0043022molecular_functionribosome binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
AASP5
AGLU19
BTHR15
BTRP43
BHOH2038
BHOH2054
BHOH2087

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
ChainResidueDetails
BHIS58

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
ChainResidueDetails
BGLU62

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:11741540
ChainResidueDetails
BARG90

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642
ChainResidueDetails
BASP55

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1jch
ChainResidueDetails
BARG90
BHIS58
BGLU62
BASP55

site_idMCSA1
Number of Residues4
DetailsM-CSA 530
ChainResidueDetails
BASP55electrostatic stabiliser, increase acidity
BHIS58promote heterolysis, proton acceptor, proton donor
BGLU62increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
BARG90electrostatic stabiliser

237735

PDB entries from 2025-06-18

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