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2IXV

Crystal structure of the modular Cpl-1 endolysin complexed with a peptidoglycan analogue (E94Q mutant)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0005515molecular_functionprotein binding
A0009253biological_processpeptidoglycan catabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00953
Number of Residues34
DetailsGLYCOSYL_HYDROL_F25_1 Glycosyl hydrolases family 25 active site signature. DVsshNGyditgileqm.....GttntIIKiSESttYlN
ChainResidueDetails
AASP10-ASN43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01252
ChainResidueDetails
AASP10
AASP92
AGLN94

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1oba
ChainResidueDetails
AASP10
AASP182
AASP92
AGLN94

site_idMCSA1
Number of Residues4
DetailsM-CSA 774
ChainResidueDetails
AASP10activator, electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor
AASP92proton donor
AGLN94activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AASP182proton acceptor

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PDB entries from 2024-05-01

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