3SQC
SQUALENE-HOPENE CYCLASE
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 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 | 3 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P48449 |
Chain | Residue | Details |
A | ASP377 | |
B | ASP377 | |
C | ASP377 |
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 | CYS376 | |
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 | CYS376 | |
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 | CYS376 | |
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 | TYR46 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
A | THR378 | modifies pKa |
A | ASP421 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
A | VAL452 | electrostatic stabiliser, hydrogen bond donor |
A | GLY490 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
A | GLY496 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | PRO602 | electrostatic stabiliser, van der waals interaction |
A | TYR606 | electrostatic stabiliser, van der waals interaction |
A | THR610 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
A | ALA94 | modifies pKa |
A | VAL128 | modifies pKa |
A | ALA170 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
A | PRO263 | modifies pKa |
A | ASP313 | electrostatic stabiliser |
A | GLN366 | electrostatic stabiliser, van der waals interaction |
A | VAL375 | modifies pKa |
A | ASP377 | 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 | TYR46 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
B | THR378 | modifies pKa |
B | ASP421 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
B | VAL452 | electrostatic stabiliser, hydrogen bond donor |
B | GLY490 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
B | GLY496 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | PRO602 | electrostatic stabiliser, van der waals interaction |
B | TYR606 | electrostatic stabiliser, van der waals interaction |
B | THR610 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
B | ALA94 | modifies pKa |
B | VAL128 | modifies pKa |
B | ALA170 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
B | PRO263 | modifies pKa |
B | ASP313 | electrostatic stabiliser |
B | GLN366 | electrostatic stabiliser, van der waals interaction |
B | VAL375 | modifies pKa |
B | ASP377 | 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 | TYR46 | hydrogen bond acceptor, increase basicity, increase nucleophilicity, modifies pKa, proton acceptor |
C | THR378 | modifies pKa |
C | ASP421 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
C | VAL452 | electrostatic stabiliser, hydrogen bond donor |
C | GLY490 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
C | GLY496 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | PRO602 | electrostatic stabiliser, van der waals interaction |
C | TYR606 | electrostatic stabiliser, van der waals interaction |
C | THR610 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
C | ALA94 | modifies pKa |
C | VAL128 | modifies pKa |
C | ALA170 | electrostatic stabiliser, polar/non-polar interaction, van der waals interaction |
C | PRO263 | modifies pKa |
C | ASP313 | electrostatic stabiliser |
C | GLN366 | electrostatic stabiliser, van der waals interaction |
C | VAL375 | modifies pKa |
C | ASP377 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |