3W7F
Crystal structure of the C(30) carotenoid dehydrosqualene synthase from staphylococcus aureus complexed with farnesyl thiopyrophosphate
Replaces: 2ZCPFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004311 | molecular_function | farnesyltranstransferase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016117 | biological_process | carotenoid biosynthetic process |
A | 0016120 | biological_process | carotene biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0016767 | molecular_function | geranylgeranyl-diphosphate geranylgeranyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046905 | molecular_function | 15-cis-phytoene synthase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004311 | molecular_function | farnesyltranstransferase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0016117 | biological_process | carotenoid biosynthetic process |
B | 0016120 | biological_process | carotene biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0016767 | molecular_function | geranylgeranyl-diphosphate geranylgeranyltransferase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0046905 | molecular_function | 15-cis-phytoene synthase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FPS A 301 |
Chain | Residue |
A | TYR41 |
A | FPS302 |
A | MG303 |
A | MG304 |
A | MG305 |
A | HOH401 |
A | HOH402 |
A | HOH403 |
A | HOH405 |
A | HOH406 |
A | HOH407 |
A | CYS44 |
A | ARG45 |
A | ASP48 |
A | VAL137 |
A | LEU141 |
A | ASN168 |
A | ARG171 |
A | ASP172 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE FPS A 302 |
Chain | Residue |
A | HIS18 |
A | SER19 |
A | LYS20 |
A | SER21 |
A | PHE22 |
A | TYR41 |
A | ARG45 |
A | ALA157 |
A | GLN165 |
A | ARG171 |
A | TYR248 |
A | ARG265 |
A | FPS301 |
A | MG304 |
A | HOH407 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 303 |
Chain | Residue |
A | ASN168 |
A | ASP172 |
A | FPS301 |
A | HOH402 |
A | HOH403 |
A | HOH408 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 304 |
Chain | Residue |
A | FPS301 |
A | FPS302 |
A | HOH406 |
A | HOH407 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 305 |
Chain | Residue |
A | ASP48 |
A | ASP52 |
A | FPS301 |
A | HOH401 |
A | HOH404 |
A | HOH405 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE FPS B 301 |
Chain | Residue |
B | PHE26 |
B | TYR41 |
B | CYS44 |
B | ARG45 |
B | ASP48 |
B | ASN168 |
B | ARG171 |
B | ASP172 |
B | FPS302 |
B | MG303 |
B | MG304 |
B | MG305 |
B | HOH401 |
B | HOH402 |
B | HOH403 |
B | HOH404 |
B | HOH405 |
B | HOH408 |
B | HOH409 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE FPS B 302 |
Chain | Residue |
B | SER19 |
B | LYS20 |
B | SER21 |
B | PHE22 |
B | TYR41 |
B | ARG45 |
B | LEU145 |
B | ALA157 |
B | LEU160 |
B | GLY161 |
B | ARG171 |
B | PHE233 |
B | TYR248 |
B | ARG265 |
B | FPS301 |
B | MG304 |
B | HOH403 |
B | HOH408 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 303 |
Chain | Residue |
B | ASN168 |
B | ASP172 |
B | FPS301 |
B | HOH404 |
B | HOH406 |
B | HOH409 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 304 |
Chain | Residue |
B | FPS301 |
B | FPS302 |
B | HOH403 |
B | HOH408 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 305 |
Chain | Residue |
B | FPS301 |
B | HOH401 |
B | HOH407 |
B | HOH574 |
B | ASP48 |
B | ASP52 |
Functional Information from PROSITE/UniProt
site_id | PS01044 |
Number of Residues | 16 |
Details | SQUALEN_PHYTOEN_SYN_1 Squalene and phytoene synthases signature 1. YCygVAGTVGevLtpI |
Chain | Residue | Details |
A | TYR129-ILE144 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F |
Chain | Residue | Details |
A | HIS18 | |
A | TYR41 | |
B | HIS18 | |
B | TYR41 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F |
Chain | Residue | Details |
A | ARG45 | |
B | ARG45 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F |
Chain | Residue | Details |
A | ASP48 | |
A | ASP52 | |
B | ASP48 | |
B | ASP52 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR |
Chain | Residue | Details |
A | GLN165 | |
B | GLN165 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR, ECO:0007744|PDB:3W7F |
Chain | Residue | Details |
A | ASN168 | |
A | ASP172 | |
B | ASN168 | |
B | ASP172 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:3W7F |
Chain | Residue | Details |
A | ARG171 | |
A | TYR248 | |
B | ARG171 | |
B | TYR248 |