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 | 0004310 | molecular_function | farnesyl-diphosphate farnesyltransferase activity |
| A | 0004311 | molecular_function | farnesyltranstransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016117 | biological_process | carotenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004310 | molecular_function | farnesyl-diphosphate farnesyltransferase activity |
| B | 0004311 | molecular_function | farnesyltranstransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016117 | biological_process | carotenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0046872 | molecular_function | metal ion binding |
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 |
