3AE0
Crystal structure of the C(30) carotenoid dehydrosqualene synthase from Staphylococcus aureus complexed with geranylgeranyl thiopyrophosphate
Functional 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 | 20 |
Details | BINDING SITE FOR RESIDUE GGS A 1001 |
Chain | Residue |
A | HIS18 |
A | LEU160 |
A | GLY161 |
A | LEU164 |
A | GLN165 |
A | ASN168 |
A | ARG171 |
A | ILE241 |
A | TYR248 |
A | ARG265 |
A | GGS1002 |
A | SER19 |
A | MG1006 |
A | LYS20 |
A | SER21 |
A | PHE22 |
A | TYR41 |
A | ARG45 |
A | LEU141 |
A | LEU145 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GGS A 1002 |
Chain | Residue |
A | MET15 |
A | TYR41 |
A | ARG45 |
A | ASP48 |
A | GLN165 |
A | ASN168 |
A | ARG171 |
A | ASP172 |
A | HOH501 |
A | HOH529 |
A | HOH535 |
A | HOH560 |
A | GGS1001 |
A | MG1005 |
A | MG1006 |
A | MG1007 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 1005 |
Chain | Residue |
A | ASN168 |
A | ASP172 |
A | HOH501 |
A | HOH529 |
A | HOH565 |
A | GGS1002 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1006 |
Chain | Residue |
A | ARG265 |
A | HOH560 |
A | GGS1001 |
A | GGS1002 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1007 |
Chain | Residue |
A | ASP48 |
A | ASP49 |
A | ASP52 |
A | HOH535 |
A | GGS1002 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GGS B 1003 |
Chain | Residue |
B | HIS18 |
B | SER19 |
B | LYS20 |
B | SER21 |
B | PHE22 |
B | TYR41 |
B | ARG45 |
B | ALA157 |
B | LEU160 |
B | GLY161 |
B | LEU164 |
B | GLN165 |
B | ASN168 |
B | ARG171 |
B | ILE241 |
B | TYR248 |
B | ARG265 |
B | GGS1004 |
B | MG1009 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GGS B 1004 |
Chain | Residue |
B | MET15 |
B | TYR41 |
B | ARG45 |
B | ASP48 |
B | LEU141 |
B | GLN165 |
B | ASN168 |
B | ARG171 |
B | ASP172 |
B | ARG265 |
B | HOH504 |
B | HOH508 |
B | HOH566 |
B | GGS1003 |
B | MG1008 |
B | MG1009 |
B | MG1010 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1008 |
Chain | Residue |
B | ASN168 |
B | ASP172 |
B | HOH504 |
B | HOH566 |
B | HOH567 |
B | GGS1004 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1009 |
Chain | Residue |
B | ARG265 |
B | GGS1003 |
B | GGS1004 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1010 |
Chain | Residue |
B | ASP48 |
B | ASP52 |
B | GGS1004 |
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 |