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 |