Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004540 | molecular_function | RNA nuclease activity |
A | 0005576 | cellular_component | extracellular region |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050830 | biological_process | defense response to Gram-positive bacterium |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004518 | molecular_function | nuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004540 | molecular_function | RNA nuclease activity |
B | 0005576 | cellular_component | extracellular region |
B | 0016787 | molecular_function | hydrolase activity |
B | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 401 |
Chain | Residue |
B | ILE44 |
B | CIT502 |
B | HOH514 |
B | HOH531 |
B | HOH643 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 402 |
Chain | Residue |
A | GLN73 |
A | THR93 |
A | HOH629 |
A | HOH647 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 403 |
Chain | Residue |
B | THR71 |
B | CIT503 |
B | HOH526 |
B | HOH541 |
B | HOH567 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CIT A 501 |
Chain | Residue |
A | LYS14 |
A | HIS15 |
A | ASN45 |
A | THR46 |
A | HIS107 |
A | PHE108 |
A | HOH504 |
A | HOH518 |
A | HOH529 |
A | HOH537 |
A | HOH547 |
A | HOH557 |
B | CIT502 |
B | HOH534 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CIT B 502 |
Chain | Residue |
A | CIT501 |
A | HOH518 |
A | HOH544 |
B | LYS14 |
B | HIS15 |
B | ASN45 |
B | THR46 |
B | PHE108 |
B | NA401 |
B | HOH506 |
B | HOH534 |
B | HOH544 |
B | HOH550 |
B | HOH570 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CIT B 503 |
Chain | Residue |
B | GLU57 |
B | ARG60 |
B | SER70 |
B | THR71 |
B | GLN72 |
B | NA403 |
B | HOH541 |
B | HOH611 |
Functional Information from PROSITE/UniProt
site_id | PS00127 |
Number of Residues | 7 |
Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpiNTF |
Chain | Residue | Details |
A | CYS41-PHE47 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P11916","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P11916","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11916","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17560606","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | HIS107 | |
A | HIS15 | |
A | LYS42 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | HIS107 | |
B | HIS15 | |
B | LYS42 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
A | HIS107 | |
A | HIS15 | |
A | LYS42 | |
A | PHE108 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1rbn |
Chain | Residue | Details |
B | HIS107 | |
B | HIS15 | |
B | LYS42 | |
B | PHE108 | |