4F6X
Crystal structure of dehydrosqualene synthase (crtm) from s. aureus complexed with bph-1112
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ZYL A 301 |
| Chain | Residue |
| A | HIS18 |
| A | TYR248 |
| A | MG303 |
| A | MG304 |
| A | HOH402 |
| A | HOH403 |
| A | PHE22 |
| A | ALA134 |
| A | VAL137 |
| A | ALA157 |
| A | LEU160 |
| A | GLN165 |
| A | ASN168 |
| A | PHE233 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | ASN168 |
| A | ASP172 |
| A | HOH401 |
| A | HOH402 |
| A | HOH403 |
| A | HOH561 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 303 |
| Chain | Residue |
| A | VAL133 |
| A | GLN165 |
| A | ZYL301 |
| A | HOH571 |
| A | HOH573 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 304 |
| Chain | Residue |
| A | ARG171 |
| A | TYR248 |
| A | ZYL301 |
| A | TAR305 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TAR A 305 |
| Chain | Residue |
| A | HIS18 |
| A | SER19 |
| A | LYS20 |
| A | SER21 |
| A | ARG171 |
| A | ARG265 |
| A | MG304 |
| A | HOH449 |
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 site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZCS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2ZCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZCR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZCQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZCR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3W7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18276850","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3W7F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
