1UCC
Crystal structure of the Ribonuclease MC1 from bitter gourd seeds complexed with 3'-UMP.
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 PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE U3P A 300 |
| Chain | Residue |
| A | GLN9 |
| A | ASN71 |
| A | VAL72 |
| A | LEU73 |
| A | PHE80 |
| A | HIS83 |
| A | LYS87 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | HIS34 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:10964705, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | TRP85 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | GLY89 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCC, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | GLN9 | |
| A | VAL72 | |
| A | HIS88 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | HIS34 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | ALA75 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | TRP81 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H |
| Chain | Residue | Details |
| A | GLU84 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 9 |
| Details | SITE: Involved in thermostability => ECO:0000269|PubMed:15322360 |
| Chain | Residue | Details |
| A | PHE102 | |
| A | LYS103 | |
| A | VAL106 | |
| A | ASN126 | |
| A | ARG128 | |
| A | LYS145 | |
| A | VAL163 | |
| A | VAL166 |
