1SQC
SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA A 667 |
| Chain | Residue |
| A | TRP312 |
| A | ASP374 |
| A | ASP376 |
| A | ASP377 |
| A | TYR420 |
| site_id | LDA |
| Number of Residues | 1 |
| Details | THE ACTIVE SITE IS LOCATED IN A LARGE CENTRAL CAVITY, AS DEFINED BY THE INHIBITOR (LDA)BINDING SITE. |
| Chain | Residue |
| A | LDA667 |
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 | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P48449 |
| Chain | Residue | Details |
| A | 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 | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | TYR493 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1d8d |
| Chain | Residue | Details |
| A | TYR545 |
| site_id | CSA4 |
| 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 | 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 |
