4EA0
Crystal structure of dehydrosqualene synthase (Crtm) from S. aureus complexed with diphosphate and quinuclidine BPH-651
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004311 | molecular_function | geranylgeranyl diphosphate synthase 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 |
| A | 0051996 | molecular_function | squalene synthase [NAD(P)H] activity |
| B | 0004311 | molecular_function | geranylgeranyl diphosphate synthase 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 |
| B | 0051996 | molecular_function | squalene synthase [NAD(P)H] activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ARG45 |
| A | ASP48 |
| A | ASP52 |
| A | MG303 |
| A | POP304 |
| A | HOH422 |
| A | HOH427 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | POP304 |
| A | HOH403 |
| A | HOH404 |
| A | ASN168 |
| A | ASP172 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 303 |
| Chain | Residue |
| A | ASP48 |
| A | ASP52 |
| A | MG301 |
| A | POP304 |
| A | HOH401 |
| A | HOH402 |
| A | HOH487 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE POP A 304 |
| Chain | Residue |
| A | ARG45 |
| A | ASP48 |
| A | ASP52 |
| A | GLN165 |
| A | ASN168 |
| A | ASP172 |
| A | MG301 |
| A | MG302 |
| A | MG303 |
| A | 651306 |
| A | HOH402 |
| A | HOH403 |
| A | HOH404 |
| A | HOH405 |
| A | HOH422 |
| A | HOH427 |
| A | HOH487 |
| A | HOH503 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TLA A 305 |
| Chain | Residue |
| A | HIS18 |
| A | SER19 |
| A | LYS20 |
| A | SER21 |
| A | ARG171 |
| A | TYR248 |
| A | ARG265 |
| A | HOH503 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 651 A 306 |
| Chain | Residue |
| A | PHE22 |
| A | ARG45 |
| A | ASP48 |
| A | VAL133 |
| A | ALA134 |
| A | GLY138 |
| A | GLY161 |
| A | LEU164 |
| A | GLN165 |
| A | POP304 |
| A | HOH501 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | ASN168 |
| B | ASP172 |
| B | POP304 |
| B | HOH406 |
| B | HOH444 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ASP48 |
| B | ASP52 |
| B | MG303 |
| B | POP304 |
| B | HOH401 |
| B | HOH402 |
| B | HOH424 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 303 |
| Chain | Residue |
| B | ARG45 |
| B | ASP48 |
| B | ASP52 |
| B | MG302 |
| B | POP304 |
| B | HOH429 |
| B | HOH482 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE POP B 304 |
| Chain | Residue |
| B | ARG45 |
| B | ASP48 |
| B | ASP52 |
| B | GLN165 |
| B | ASN168 |
| B | ASP172 |
| B | ARG265 |
| B | MG301 |
| B | MG302 |
| B | MG303 |
| B | 651305 |
| B | HOH401 |
| B | HOH415 |
| B | HOH424 |
| B | HOH427 |
| B | HOH429 |
| B | HOH444 |
| B | HOH482 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 651 B 305 |
| Chain | Residue |
| B | GLY138 |
| B | LEU164 |
| B | GLN165 |
| B | POP304 |
| B | PHE22 |
| B | ARG45 |
| B | ASP48 |
| B | VAL133 |
| B | ALA134 |
| B | VAL137 |
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 |
