5JMG
X-ray structure of the complex between bovine pancreatic ribonuclease and pentachlorocarbonyliridate(III) (4 days of soaking)
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 IR A 201 |
| Chain | Residue |
| A | HIS105 |
| A | CL202 |
| A | CMO203 |
| A | HOH381 |
| A | HOH392 |
| A | HOH394 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 202 |
| Chain | Residue |
| A | HOH381 |
| A | HIS105 |
| A | IR201 |
| A | CMO203 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CMO A 203 |
| Chain | Residue |
| A | IR201 |
| A | CL202 |
| A | HOH381 |
| A | HOH394 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue IR A 204 |
| Chain | Residue |
| A | MET29 |
| A | CMO205 |
| A | HOH367 |
| A | HOH389 |
| A | HOH409 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CMO A 205 |
| Chain | Residue |
| A | MET29 |
| A | SER32 |
| A | ARG33 |
| A | IR204 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue IR A 206 |
| Chain | Residue |
| A | LYS1 |
| A | ARG85 |
| A | CL207 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 207 |
| Chain | Residue |
| A | ARG85 |
| A | IR206 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue IR A 208 |
| Chain | Residue |
| A | GLU111 |
| A | HIS119 |
| A | HOH315 |
| A | HOH362 |
| A | HOH369 |
| A | HOH395 |
| A | HOH401 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue IR B 201 |
| Chain | Residue |
| B | HIS119 |
| B | CL202 |
| B | CMO203 |
| B | HOH351 |
| B | HOH380 |
| B | HOH409 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 202 |
| Chain | Residue |
| A | GLN69 |
| B | ASN71 |
| B | GLU111 |
| B | HIS119 |
| B | IR201 |
| B | CMO203 |
| B | HOH380 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue CMO B 203 |
| Chain | Residue |
| A | GLN69 |
| A | THR70 |
| B | GLU111 |
| B | IR201 |
| B | CL202 |
| B | HOH351 |
| B | HOH380 |
| B | HOH409 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 204 |
| Chain | Residue |
| B | HIS119 |
| B | CL205 |
| B | HOH417 |
| B | HOH429 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 205 |
| Chain | Residue |
| B | CL204 |
| B | HOH429 |
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 |
