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1IOO

CRYSTAL STRUCTURE OF NICOTIANA ALATA GEMETOPHYTIC SELF-INCOMPATIBILITY ASSOCIATED SF11-RNASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0005576cellular_componentextracellular region
A0006401biological_processRNA catabolic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0033897molecular_functionribonuclease T2 activity
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
B0005576cellular_componentextracellular region
B0006401biological_processRNA catabolic process
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0033897molecular_functionribonuclease T2 activity
Functional Information from PROSITE/UniProt
site_idPS00530
Number of Residues8
DetailsRNASE_T2_1 Ribonuclease T2 family histidine active site 1. FtIHGLWP
ChainResidueDetails
APHE29-PRO36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSignal: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10045","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724536","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"P08056","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10045","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724536","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P23540","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11724536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IOO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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