3VJA
Crystal structure of the 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NI A 401 |
| Chain | Residue |
| A | HIS98 |
| A | GLU343 |
| A | HIS347 |
| A | HOH455 |
| A | HOH466 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NI B 401 |
| Chain | Residue |
| B | HIS98 |
| B | GLU343 |
| B | HIS347 |
| B | HOH451 |
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 | 40 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | SER284-TYR304 | |
| B | SER284-TYR304 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24531458 |
| Chain | Residue | Details |
| A | ARG52 | |
| B | 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 | 6 |
| 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 |
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 |
