3ADZ
Crystal structure of the C(30) carotenoid dehydrosqualene synthase from Staphylococcus aureus complexed with intermediate PSPP
Functional 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 | 0016767 | molecular_function | geranylgeranyl-diphosphate geranylgeranyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046905 | molecular_function | 15-cis-phytoene synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PS7 A 1001 |
| Chain | Residue |
| A | HIS18 |
| A | LEU164 |
| A | ASN168 |
| A | ARG171 |
| A | TYR248 |
| A | ARG265 |
| A | HOH517 |
| A | HOH532 |
| A | HOH582 |
| A | HOH596 |
| A | HOH723 |
| A | SER19 |
| A | MG1003 |
| A | PHE26 |
| A | TYR41 |
| A | CYS44 |
| A | ARG45 |
| A | VAL133 |
| A | VAL137 |
| A | ALA157 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1002 |
| Chain | Residue |
| A | ASN168 |
| A | ASP172 |
| A | HOH504 |
| A | HOH576 |
| A | HOH593 |
| A | HOH640 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1003 |
| Chain | Residue |
| A | HIS18 |
| A | HOH532 |
| A | HOH664 |
| A | PS71001 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCS, ECO:0007744|PDB:3W7F |
| Chain | Residue | Details |
| A | HIS18 | |
| A | TYR41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F |
| Chain | Residue | Details |
| A | ARG45 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:3W7F |
| Chain | Residue | Details |
| A | ASP52 | |
| A | ASP48 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR |
| Chain | Residue | Details |
| A | GLN165 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18276850, ECO:0007744|PDB:2ZCQ, ECO:0007744|PDB:2ZCR, ECO:0007744|PDB:3W7F |
| Chain | Residue | Details |
| A | ASP172 | |
| A | ASN168 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:18276850, ECO:0007744|PDB:3W7F |
| Chain | Residue | Details |
| A | ARG171 | |
| A | TYR248 |
