3BCP
Crystal Structure of The Swapped non covalent form of P19A/L28Q/N67D BS-RNase
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 | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050830 | biological_process | defense response to Gram-positive bacterium |
| A | 0051607 | biological_process | defense response to virus |
| 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 | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
| B | 0051607 | biological_process | defense response to virus |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0004522 | molecular_function | ribonuclease A activity |
| C | 0004540 | molecular_function | RNA nuclease activity |
| C | 0005576 | cellular_component | extracellular region |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050830 | biological_process | defense response to Gram-positive bacterium |
| C | 0051607 | biological_process | defense response to virus |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0004522 | molecular_function | ribonuclease A activity |
| D | 0004540 | molecular_function | RNA nuclease activity |
| D | 0005576 | cellular_component | extracellular region |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0050830 | biological_process | defense response to Gram-positive bacterium |
| D | 0051607 | biological_process | defense response to virus |
Functional Information from PROSITE/UniProt
| site_id | PS00127 |
| Number of Residues | 7 |
| Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
| Chain | Residue | Details |
| A | CYS40-PHE46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS12 | |
| B | HIS12 | |
| C | HIS12 | |
| D | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 | |
| B | HIS119 | |
| C | HIS119 | |
| D | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS7 | |
| B | ARG85 | |
| C | LYS7 | |
| C | ARG10 | |
| C | LYS41 | |
| C | LYS66 | |
| C | ARG85 | |
| D | LYS7 | |
| D | ARG10 | |
| D | LYS41 | |
| D | LYS66 | |
| A | ARG10 | |
| D | ARG85 | |
| A | LYS41 | |
| A | LYS66 | |
| A | ARG85 | |
| B | LYS7 | |
| B | ARG10 | |
| B | LYS41 | |
| B | LYS66 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine; by deterioration => ECO:0000269|PubMed:2057997 |
| Chain | Residue | Details |
| A | ASP67 | |
| B | ASP67 | |
| C | ASP67 | |
| D | ASP67 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| A | PHE120 | |
| A | HIS119 | |
| A | HIS12 | |
| A | LYS41 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| B | PHE120 | |
| B | HIS119 | |
| B | HIS12 | |
| B | LYS41 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| C | PHE120 | |
| C | HIS119 | |
| C | HIS12 | |
| C | LYS41 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| D | PHE120 | |
| D | HIS119 | |
| D | HIS12 | |
| D | LYS41 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| A | HIS119 | |
| A | HIS12 | |
| A | LYS41 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| B | HIS119 | |
| B | HIS12 | |
| B | LYS41 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| C | HIS119 | |
| C | HIS12 | |
| C | LYS41 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| D | HIS119 | |
| D | HIS12 | |
| D | LYS41 |
