1GSZ
Crystal Structure of a Squalene Cyclase in Complex with the Potential Anticholesteremic Drug Ro48-8071
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005811 | cellular_component | lipid droplet |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0016104 | biological_process | triterpenoid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016866 | molecular_function | intramolecular transferase activity |
| A | 0051007 | molecular_function | squalene-hopene cyclase activity |
| B | 0005811 | cellular_component | lipid droplet |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0016104 | biological_process | triterpenoid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016866 | molecular_function | intramolecular transferase activity |
| B | 0051007 | molecular_function | squalene-hopene cyclase activity |
| C | 0005811 | cellular_component | lipid droplet |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0016104 | biological_process | triterpenoid biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016866 | molecular_function | intramolecular transferase activity |
| C | 0051007 | molecular_function | squalene-hopene cyclase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE C8E A 1629 |
| Chain | Residue |
| A | ARG251 |
| A | PRO348 |
| A | GLY349 |
| A | ASP350 |
| A | VAL353 |
| B | ARG238 |
| B | ILE242 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE R71 A 1630 |
| Chain | Residue |
| A | ILE261 |
| A | PRO263 |
| A | TRP312 |
| A | ASP376 |
| A | TRP489 |
| A | PHE601 |
| A | PHE605 |
| A | TYR609 |
| A | TRP169 |
| A | THR173 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C8E B 1629 |
| Chain | Residue |
| A | ARG183 |
| A | ARG238 |
| A | ILE242 |
| B | ARG251 |
| B | GLY349 |
| B | ASP350 |
| B | VAL353 |
| B | TYR371 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE R71 B 1630 |
| Chain | Residue |
| B | ALA170 |
| B | THR173 |
| B | ILE261 |
| B | PRO263 |
| B | TRP312 |
| B | ASP374 |
| B | ASP376 |
| B | PHE437 |
| B | TRP489 |
| B | PHE601 |
| B | TYR609 |
| B | HOH2057 |
| B | HOH2061 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE C8E C 1629 |
| Chain | Residue |
| C | ARG238 |
| C | ILE242 |
| C | ARG251 |
| C | PRO348 |
| C | GLY349 |
| C | ASP350 |
| C | TYR371 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE R71 C 1630 |
| Chain | Residue |
| C | TRP169 |
| C | ALA170 |
| C | THR173 |
| C | ILE261 |
| C | PRO263 |
| C | TRP312 |
| C | ASP374 |
| C | ASP376 |
| C | ASP377 |
| C | TYR420 |
| C | TRP489 |
| C | PHE601 |
| C | PHE605 |
| C | TYR609 |
| C | HOH2081 |
Functional Information from PROSITE/UniProt
| site_id | PS01074 |
| Number of Residues | 15 |
| Details | TERPENE_SYNTHASES Terpene synthases signature. DGSWfGrWGVnYlYG |
| Chain | Residue | Details |
| A | ASP482-GLY496 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 123 |
| Details | Repeat: {"description":"PFTB 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 123 |
| Details | Repeat: {"description":"PFTB 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 123 |
| Details | Repeat: {"description":"PFTB 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 123 |
| Details | Repeat: {"description":"PFTB 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 120 |
| Details | Repeat: {"description":"PFTB 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 123 |
| Details | Repeat: {"description":"PFTB 6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 144 |
| Details | Repeat: {"description":"PFTB 7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12747780","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9931258","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | ALA364 |
| site_id | CSA10 |
| Number of Residues | 15 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | PHE605 | |
| A | TYR495 | |
| A | TRP489 | |
| A | TRP169 | |
| A | ASP376 | |
| A | GLU93 | |
| A | PHE365 | |
| A | PHE601 | |
| A | GLN262 | |
| A | ASP374 | |
| A | ASP377 | |
| A | GLU45 | |
| A | HIS451 | |
| A | ARG127 | |
| A | TRP312 |
| site_id | CSA11 |
| Number of Residues | 15 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| B | PHE605 | |
| B | TYR495 | |
| B | TRP489 | |
| B | TRP169 | |
| B | ASP376 | |
| B | GLU93 | |
| B | PHE365 | |
| B | PHE601 | |
| B | GLN262 | |
| B | ASP374 | |
| B | ASP377 | |
| B | GLU45 | |
| B | HIS451 | |
| B | ARG127 | |
| B | TRP312 |
| site_id | CSA12 |
| Number of Residues | 15 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| C | PHE605 | |
| C | TYR495 | |
| C | TRP489 | |
| C | TRP169 | |
| C | ASP376 | |
| C | GLU93 | |
| C | PHE365 | |
| C | PHE601 | |
| C | GLN262 | |
| C | ASP374 | |
| C | ASP377 | |
| C | GLU45 | |
| C | HIS451 | |
| C | ARG127 | |
| C | TRP312 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| B | ALA364 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| C | ALA364 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | TYR493 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | TYR545 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| B | TYR493 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| B | TYR545 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| C | TYR493 |
| site_id | CSA9 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| C | TYR545 |
| site_id | MCSA1 |
| Number of Residues | 17 |
| Details | M-CSA 254 |
| Chain | Residue | Details |
| A | GLU45 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
| A | ASP377 | modifies pKa |
| A | TYR420 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| A | HIS451 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP489 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| A | TYR495 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | PHE601 | electrostatic stabiliser, van der waals interaction |
| A | PHE605 | electrostatic stabiliser, van der waals interaction |
| A | TYR609 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| A | GLU93 | modifies pKa |
| A | ARG127 | modifies pKa |
| A | TRP169 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| A | GLN262 | modifies pKa |
| A | TRP312 | electrostatic stabiliser |
| A | PHE365 | electrostatic stabiliser, van der waals interaction |
| A | ASP374 | modifies pKa |
| A | ASP376 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 17 |
| Details | M-CSA 254 |
| Chain | Residue | Details |
| B | GLU45 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
| B | ASP377 | modifies pKa |
| B | TYR420 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| B | HIS451 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP489 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| B | TYR495 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | PHE601 | electrostatic stabiliser, van der waals interaction |
| B | PHE605 | electrostatic stabiliser, van der waals interaction |
| B | TYR609 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| B | GLU93 | modifies pKa |
| B | ARG127 | modifies pKa |
| B | TRP169 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| B | GLN262 | modifies pKa |
| B | TRP312 | electrostatic stabiliser |
| B | PHE365 | electrostatic stabiliser, van der waals interaction |
| B | ASP374 | modifies pKa |
| B | ASP376 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 17 |
| Details | M-CSA 254 |
| Chain | Residue | Details |
| C | GLU45 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
| C | ASP377 | modifies pKa |
| C | TYR420 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| C | HIS451 | electrostatic stabiliser, hydrogen bond donor |
| C | TRP489 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| C | TYR495 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| C | PHE601 | electrostatic stabiliser, van der waals interaction |
| C | PHE605 | electrostatic stabiliser, van der waals interaction |
| C | TYR609 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| C | GLU93 | modifies pKa |
| C | ARG127 | modifies pKa |
| C | TRP169 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
| C | GLN262 | modifies pKa |
| C | TRP312 | electrostatic stabiliser |
| C | PHE365 | electrostatic stabiliser, van der waals interaction |
| C | ASP374 | modifies pKa |
| C | ASP376 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
