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1DE3

SOLUTION STRUCTURE OF THE CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0017148biological_processnegative regulation of translation
A0033902molecular_functionrRNA endonuclease activity
A2000766biological_processnegative regulation of cytoplasmic translation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10591106, 8980143, 10843858, 9580156
ChainResidueDetails
AHIS137
AGLU96
AHIS50

site_idMCSA1
Number of Residues3
DetailsM-CSA 832
ChainResidueDetails
AHIS50electrostatic stabiliser
AGLU96increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AHIS137increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

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PDB entries from 2025-10-01

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