2G8R
The crystal structure of the RNase A- 3-N-piperidine-4-carboxyl-3-deoxy-ara-uridine complex
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 | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016829 | molecular_function | lyase activity |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016829 | molecular_function | lyase activity |
| B | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE N3E A 998 |
| Chain | Residue |
| A | ALA4 |
| A | HOH1123 |
| A | HOH1124 |
| B | ASN62 |
| B | THR70 |
| B | TYR73 |
| B | HOH218 |
| A | ASN67 |
| A | ASN71 |
| A | ALA109 |
| A | GLU111 |
| A | VAL118 |
| A | HIS119 |
| A | HOH1009 |
| A | HOH1049 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE N3E A 999 |
| Chain | Residue |
| A | HIS12 |
| A | ASN44 |
| A | THR45 |
| A | LYS66 |
| A | ASN67 |
| A | HIS119 |
| A | PHE120 |
| A | ASP121 |
| A | HOH1016 |
| A | HOH1049 |
| A | HOH1054 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS12 | |
| B | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| A | HIS119 | |
| B | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS7 | |
| B | ARG85 | |
| A | ARG10 | |
| A | LYS41 | |
| A | LYS66 | |
| A | ARG85 | |
| B | LYS7 | |
| B | ARG10 | |
| B | LYS41 | |
| B | LYS66 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761 |
| Chain | Residue | Details |
| A | LYS1 | |
| A | LYS7 | |
| A | LYS37 | |
| A | LYS41 | |
| B | LYS1 | |
| B | LYS7 | |
| B | LYS37 | |
| B | LYS41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| A | ASN34 | |
| B | ASN34 |
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 | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| A | HIS119 | |
| A | HIS12 | |
| A | LYS41 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1rbn |
| Chain | Residue | Details |
| B | HIS119 | |
| B | HIS12 | |
| B | LYS41 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| A | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| B | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
