1EZF
CRYSTAL STRUCTURE OF HUMAN SQUALENE SYNTHASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004310 | molecular_function | farnesyl-diphosphate farnesyltransferase activity |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0045338 | biological_process | farnesyl diphosphate metabolic process |
| A | 0051996 | molecular_function | squalene synthase activity |
| B | 0004310 | molecular_function | farnesyl-diphosphate farnesyltransferase activity |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0045338 | biological_process | farnesyl diphosphate metabolic process |
| B | 0051996 | molecular_function | squalene synthase activity |
| C | 0004310 | molecular_function | farnesyl-diphosphate farnesyltransferase activity |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| C | 0045338 | biological_process | farnesyl diphosphate metabolic process |
| C | 0051996 | molecular_function | squalene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE IN0 A 991 |
| Chain | Residue |
| A | ARG52 |
| A | GLN212 |
| A | PHE288 |
| A | PRO292 |
| A | HOH1075 |
| A | SER53 |
| A | PHE54 |
| A | TYR73 |
| A | ALA176 |
| A | GLY180 |
| A | LEU183 |
| A | GLY208 |
| A | LEU211 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IN0 B 992 |
| Chain | Residue |
| B | SER51 |
| B | ARG52 |
| B | SER53 |
| B | PHE54 |
| B | TYR73 |
| B | VAL179 |
| B | GLY180 |
| B | LEU183 |
| B | GLY208 |
| B | LEU211 |
| B | GLN212 |
| B | PHE288 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE IN0 C 995 |
| Chain | Residue |
| C | ARG52 |
| C | SER53 |
| C | PHE54 |
| C | TYR73 |
| C | LEU76 |
| C | GLY180 |
| C | LEU183 |
| C | MET207 |
| C | GLY208 |
| C | LEU211 |
| C | GLN212 |
| C | PHE288 |
| C | HOH1036 |
Functional Information from PROSITE/UniProt
| site_id | PS01044 |
| Number of Residues | 16 |
| Details | SQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YChyVAGLVGigLsrL |
| Chain | Residue | Details |
| A | TYR171-LEU186 |
| site_id | PS01045 |
| Number of Residues | 26 |
| Details | SQUALEN_PHYTOEN_SYN_2 Squalene and phytoene synthases signature 2. MGlflQkt.NIiRDYleDqqgg...ReFwP |
| Chain | Residue | Details |
| A | MET207-PRO232 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | SER284-TYR304 | |
| B | SER284-TYR304 | |
| C | SER284-TYR304 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24531458 |
| Chain | Residue | Details |
| A | ARG52 | |
| B | ARG317 | |
| C | ARG52 | |
| C | ARG77 | |
| C | ARG218 | |
| C | LYS315 | |
| C | ARG317 | |
| A | ARG77 | |
| A | ARG218 | |
| A | LYS315 | |
| A | ARG317 | |
| B | ARG52 | |
| B | ARG77 | |
| B | ARG218 | |
| B | LYS315 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24531458, ECO:0007744|PDB:3WEG, ECO:0007744|PDB:3WEH |
| Chain | Residue | Details |
| A | ASP80 | |
| A | GLU83 | |
| A | ASP84 | |
| B | ASP80 | |
| B | GLU83 | |
| B | ASP84 | |
| C | ASP80 | |
| C | GLU83 | |
| C | ASP84 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 264 |
| Chain | Residue | Details |
| A | TYR171 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG218 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| A | ARG228 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| A | PHE288 | polar/non-polar interaction, steric role, van der waals interaction |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 264 |
| Chain | Residue | Details |
| B | TYR171 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG218 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| B | ARG228 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| B | PHE288 | polar/non-polar interaction, steric role, van der waals interaction |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 264 |
| Chain | Residue | Details |
| C | TYR171 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG218 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| C | ARG228 | electrostatic stabiliser, hydrogen bond donor, promote heterolysis |
| C | PHE288 | polar/non-polar interaction, steric role, van der waals interaction |
