6XVX
X-ray structure obtained upon reaction of dirhodium tetraacetate with RNase A (high resolution)
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 | |
BBB | ARG85 | |
AAA | ARG10 | |
AAA | LYS41 | |
AAA | LYS66 | |
AAA | ARG85 | |
BBB | LYS7 | |
BBB | ARG10 | |
BBB | LYS41 | |
BBB | 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 |
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 |