Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004522 | molecular_function | ribonuclease A activity |
| A | 0004540 | molecular_function | RNA nuclease activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0019731 | biological_process | antibacterial humoral response |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0004522 | molecular_function | ribonuclease A activity |
| B | 0004540 | molecular_function | RNA nuclease activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0019731 | biological_process | antibacterial humoral response |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE UM3 A 301 |
| Chain | Residue |
| A | ARG7 |
| A | GLY119 |
| A | HOH333 |
| A | GLN11 |
| A | HIS12 |
| A | LYS40 |
| A | PHE42 |
| A | ASN43 |
| A | THR44 |
| A | ARG101 |
| A | PHE117 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UM3 B 302 |
| Chain | Residue |
| B | HIS12 |
| B | PHE42 |
| B | ASN43 |
| B | THR44 |
| B | ARG101 |
| B | PHE117 |
| B | GLY119 |
Functional Information from PROSITE/UniProt
| site_id | PS00127 |
| Number of Residues | 7 |
| Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKrfNTF |
| Chain | Residue | Details |
| A | CYS39-PHE45 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS12 | |
| B | HIS12 | |
| Chain | Residue | Details |
| A | HIS116 | |
| B | HIS116 | |
| Chain | Residue | Details |
| A | ARG7 | |
| B | ASN43 | |
| B | THR44 | |
| B | PHE117 | |
| A | HIS12 | |
| A | LYS40 | |
| A | ASN43 | |
| A | THR44 | |
| A | PHE117 | |
| B | ARG7 | |
| B | HIS12 | |
| B | LYS40 | |
| Chain | Residue | Details |
| A | GLN1 | |
| B | GLN1 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 9878400 |
| Chain | Residue | Details |
| A | LYS40 | |
| A | HIS116 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 693 |
| Chain | Residue | Details |
| A | HIS12 | proton acceptor, proton donor |
| A | LYS40 | electrostatic stabiliser |
| A | HIS116 | proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 693 |
| Chain | Residue | Details |
| B | HIS12 | proton acceptor, proton donor |
| B | LYS40 | electrostatic stabiliser |
| B | HIS116 | proton acceptor, proton donor |
