7R1P
X-ray structure of the adduct formed upon reaction of the gold(I) N-heterocyclic carbene complex Au1 with RNase A
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0003676 | molecular_function | nucleic acid binding |
| AAA | 0004519 | molecular_function | endonuclease activity |
| AAA | 0004522 | molecular_function | ribonuclease A activity |
| AAA | 0004540 | molecular_function | RNA nuclease activity |
| AAA | 0005515 | molecular_function | protein binding |
| AAA | 0005576 | cellular_component | extracellular region |
| AAA | 0016829 | molecular_function | lyase activity |
| AAA | 0050830 | biological_process | defense response to Gram-positive bacterium |
| BBB | 0003676 | molecular_function | nucleic acid binding |
| BBB | 0004519 | molecular_function | endonuclease activity |
| BBB | 0004522 | molecular_function | ribonuclease A activity |
| BBB | 0004540 | molecular_function | RNA nuclease activity |
| BBB | 0005515 | molecular_function | protein binding |
| BBB | 0005576 | cellular_component | extracellular region |
| BBB | 0016829 | molecular_function | lyase activity |
| BBB | 0050830 | biological_process | defense response to Gram-positive bacterium |
Functional Information from PROSITE/UniProt
| site_id | PS00127 |
| Number of Residues | 7 |
| Details | RNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF |
| Chain | Residue | Details |
| AAA | CYS40-PHE46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| AAA | HIS12 | |
| BBB | HIS12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor |
| Chain | Residue | Details |
| AAA | HIS119 | |
| BBB | HIS119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| AAA | LYS7 | |
| AAA | ARG10 | |
| BBB | LYS66 | |
| BBB | ARG85 | |
| AAA | LYS41 | |
| AAA | LYS66 | |
| AAA | ARG85 | |
| BBB | LYS7 | |
| BBB | ARG10 | |
| BBB | LYS41 |
| 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 |
| AAA | LYS1 | |
| AAA | LYS7 | |
| AAA | LYS37 | |
| AAA | LYS41 | |
| BBB | LYS1 | |
| BBB | LYS7 | |
| BBB | LYS37 | |
| BBB | LYS41 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553 |
| Chain | Residue | Details |
| AAA | ASN34 | |
| BBB | ASN34 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| AAA | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| AAA | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| AAA | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| AAA | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| AAA | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 164 |
| Chain | Residue | Details |
| BBB | HIS12 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| BBB | LYS41 | electrostatic stabiliser, hydrogen bond donor |
| BBB | HIS119 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| BBB | PHE120 | electrostatic stabiliser, hydrogen bond donor |
| BBB | ASP121 | electrostatic stabiliser, hydrogen bond acceptor |
