4S18
The X-ray structure of the adduct formed in the reaction between bovine pancreatic ribonuclease and oxaliplatin
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 | 6 |
Details | BINDING SITE FOR RESIDUE 1PT A 201 |
Chain | Residue |
A | VAL118 |
A | HIS119 |
A | HOH301 |
A | HOH310 |
A | HOH311 |
A | HOH316 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PT A 202 |
Chain | Residue |
A | GLN101 |
A | ASP14 |
A | TYR25 |
A | MET29 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 1PT A 203 |
Chain | Residue |
A | HIS105 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PT B 201 |
Chain | Residue |
B | HIS119 |
B | PHE120 |
B | HOH301 |
B | HOH341 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PT B 202 |
Chain | Residue |
B | ASP14 |
B | SER16 |
B | SER21 |
B | TYR25 |
B | MET29 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 1PT B 203 |
Chain | Residue |
B | HIS105 |
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 | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000006","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
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 |