3MX8
Crystal structure of ribonuclease A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 253 |
| Chain | Residue |
| A | HIS12 |
| A | LYS41 |
| A | VAL43 |
| A | ASN44 |
| A | THR45 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 254 |
| Chain | Residue |
| A | HOH272 |
| A | HOH292 |
| A | HOH295 |
| A | HOH296 |
| A | HOH383 |
| A | LYS1 |
| A | THR3 |
| A | ALA4 |
| A | ASN190 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 255 |
| Chain | Residue |
| A | GLN139 |
| A | HIS140 |
| A | LYS169 |
| A | HIS247 |
| A | PHE248 |
| A | HOH265 |
| A | HOH342 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 256 |
| Chain | Residue |
| A | GLN11 |
| A | HIS12 |
| A | VAL118 |
| A | HIS119 |
| A | PHE120 |
| A | HOH287 |
| A | HOH416 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 257 |
| Chain | Residue |
| A | THR131 |
| A | ALA132 |
| A | HOH280 |
| A | HOH446 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 258 |
| Chain | Residue |
| A | HIS140 |
| A | ASN172 |
| A | THR173 |
| A | HOH342 |
| A | HOH365 |
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 | |
| A | CYS168-PHE174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | 1 |
| 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 | HIS140 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | LYS169 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS247 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | PHE248 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP249 | electrostatic stabiliser, hydrogen bond acceptor |
