2E8T
S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium, FsPP and IPP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004161 | molecular_function | dimethylallyltranstransferase activity |
| A | 0004311 | molecular_function | farnesyltranstransferase activity |
| A | 0004337 | molecular_function | geranyltranstransferase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0015031 | biological_process | protein transport |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0033384 | biological_process | geranyl diphosphate biosynthetic process |
| A | 0033386 | biological_process | geranylgeranyl diphosphate biosynthetic process |
| A | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004161 | molecular_function | dimethylallyltranstransferase activity |
| B | 0004311 | molecular_function | farnesyltranstransferase activity |
| B | 0004337 | molecular_function | geranyltranstransferase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0015031 | biological_process | protein transport |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0033384 | biological_process | geranyl diphosphate biosynthetic process |
| B | 0033386 | biological_process | geranylgeranyl diphosphate biosynthetic process |
| B | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1301 |
| Chain | Residue |
| A | ASP80 |
| A | ASP84 |
| A | HOH448 |
| A | HOH532 |
| A | FPS1201 |
| A | MG1302 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1302 |
| Chain | Residue |
| A | HOH840 |
| A | FPS1201 |
| A | MG1301 |
| A | ASP80 |
| A | ASP84 |
| A | HOH839 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1303 |
| Chain | Residue |
| B | ASP80 |
| B | ASP84 |
| B | HOH824 |
| B | FPS1202 |
| B | MG1304 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1304 |
| Chain | Residue |
| B | ASP80 |
| B | ASP84 |
| B | HOH453 |
| B | FPS1202 |
| B | MG1303 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IPE A 1001 |
| Chain | Residue |
| A | ARG44 |
| A | HIS73 |
| A | ARG90 |
| A | TYR210 |
| A | GLN211 |
| A | HOH539 |
| A | HOH930 |
| A | FPS1201 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IPE B 1002 |
| Chain | Residue |
| B | LYS38 |
| B | ARG44 |
| B | HIS73 |
| B | LEU77 |
| B | ARG90 |
| B | TYR210 |
| B | GLN211 |
| B | ASP214 |
| B | HOH558 |
| B | HOH829 |
| B | FPS1202 |
| site_id | AC7 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FPS A 1201 |
| Chain | Residue |
| A | LEU72 |
| A | SER76 |
| A | LEU77 |
| A | ASP80 |
| A | ASP84 |
| A | ARG89 |
| A | TYR112 |
| A | LEU140 |
| A | LEU143 |
| A | HIS144 |
| A | GLN147 |
| A | LYS174 |
| A | LEU178 |
| A | GLN211 |
| A | ASP214 |
| A | LYS238 |
| A | HOH448 |
| A | HOH839 |
| A | IPE1001 |
| A | MG1301 |
| A | MG1302 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FPS B 1202 |
| Chain | Residue |
| B | LEU72 |
| B | SER76 |
| B | LEU77 |
| B | ASP80 |
| B | ARG89 |
| B | TYR112 |
| B | LEU140 |
| B | LEU143 |
| B | HIS144 |
| B | GLN147 |
| B | LYS174 |
| B | GLN211 |
| B | ASP214 |
| B | LYS238 |
| B | HOH447 |
| B | HOH674 |
| B | HOH824 |
| B | IPE1002 |
| B | MG1303 |
| B | MG1304 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17535895 |
| Chain | Residue | Details |
| A | LYS41 | |
| A | LYS238 | |
| B | LYS41 | |
| B | ARG44 | |
| B | HIS73 | |
| B | ARG89 | |
| B | ARG90 | |
| B | LYS174 | |
| B | THR175 | |
| B | GLN211 | |
| B | ASN218 | |
| A | ARG44 | |
| B | LYS238 | |
| A | HIS73 | |
| A | ARG89 | |
| A | ARG90 | |
| A | LYS174 | |
| A | THR175 | |
| A | GLN211 | |
| A | ASN218 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 |
| Chain | Residue | Details |
| A | ASP80 | |
| A | ASP84 | |
| B | ASP80 | |
| B | ASP84 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17535895 |
| Chain | Residue | Details |
| A | LYS228 | |
| B | LYS228 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for determining product chain length |
| Chain | Residue | Details |
| A | TYR112 | |
| B | TYR112 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fps |
| Chain | Residue | Details |
| A | TYR210 | |
| A | ARG89 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fps |
| Chain | Residue | Details |
| B | TYR210 | |
| B | ARG89 |
