5JLG
The X-ray structure of the adduct formed in the reaction between bovine pancreatic ribonuclease and compound I, a piano-stool organometallic Ru(II) arene compound containing an O,S-chelating ligand
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 | 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase 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 | 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 5 |
| Details | binding site for residue RU A 201 |
| Chain | Residue |
| A | HIS105 |
| A | 6L6202 |
| A | HOH338 |
| A | HOH396 |
| A | HOH413 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 6L6 A 202 |
| Chain | Residue |
| A | PRO114 |
| A | RU201 |
| A | HOH335 |
| A | HOH338 |
| A | HOH396 |
| A | HOH400 |
| B | ARG10 |
| B | ASN34 |
| A | GLN74 |
| A | TYR76 |
| A | HIS105 |
| A | ASN113 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 203 |
| Chain | Residue |
| A | ASN62 |
| A | VAL63 |
| A | ALA64 |
| A | THR70 |
| B | HOH321 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue RU B 201 |
| Chain | Residue |
| B | HIS105 |
| B | 6L6202 |
| B | DMS203 |
| B | DMS204 |
| B | HOH335 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue 6L6 B 202 |
| Chain | Residue |
| B | ASP83 |
| B | THR100 |
| B | ALA102 |
| B | LYS104 |
| B | HIS105 |
| B | VAL124 |
| B | RU201 |
| B | DMS203 |
| B | DMS204 |
| B | HOH335 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 203 |
| Chain | Residue |
| B | RU201 |
| B | 6L6202 |
| B | DMS204 |
| B | HOH335 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue DMS B 204 |
| Chain | Residue |
| A | ASN67 |
| B | TYR76 |
| B | HIS105 |
| B | RU201 |
| B | 6L6202 |
| B | DMS203 |
| B | HOH335 |
| B | HOH387 |
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 | 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 |
