1IQQ
Crystal Structure of Japanese pear S3-RNase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0033897 | molecular_function | ribonuclease T2 activity |
Functional Information from PROSITE/UniProt
| site_id | PS00530 |
| Number of Residues | 8 |
| Details | RNASE_T2_1 Ribonuclease T2 family histidine active site 1. FtVHGLWP |
| Chain | Residue | Details |
| A | PHE30-PRO37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10045","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11577107","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11577107","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10045","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11577107","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P23540","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10469125","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10469125","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11577107","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IQQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bol |
| Chain | Residue | Details |
| A | GLU84 | |
| A | HIS88 | |
| A | HIS33 |
