4OPD
Constructing tailored isoprenoid products by structure-guided modification of geranylgeranyl reductase.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006650 | biological_process | glycerophospholipid metabolic process |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006650 | biological_process | glycerophospholipid metabolic process |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016628 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FDA A 501 |
| Chain | Residue |
| A | ILE11 |
| A | PRO46 |
| A | CYS47 |
| A | GLY48 |
| A | ASP49 |
| A | ALA50 |
| A | THR120 |
| A | THR121 |
| A | ALA122 |
| A | ALA156 |
| A | THR157 |
| A | GLY12 |
| A | GLY158 |
| A | SER160 |
| A | SER162 |
| A | ALA185 |
| A | ALA267 |
| A | GLY287 |
| A | ASP288 |
| A | VAL293 |
| A | GLY298 |
| A | GLY299 |
| A | GLY14 |
| A | GLY300 |
| A | LYS301 |
| A | GRG502 |
| A | HOH601 |
| A | HOH606 |
| A | HOH608 |
| A | HOH609 |
| A | HOH620 |
| A | HOH625 |
| A | HOH627 |
| A | PHE15 |
| A | HOH644 |
| A | HOH655 |
| A | ALA16 |
| A | ASP35 |
| A | SER36 |
| A | LYS37 |
| A | LYS45 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GRG A 502 |
| Chain | Residue |
| A | ALA50 |
| A | SER52 |
| A | ASN90 |
| A | GLY91 |
| A | GLU92 |
| A | TYR215 |
| A | TRP217 |
| A | HIS297 |
| A | GLY298 |
| A | GLY299 |
| A | FDA501 |
| A | GRG503 |
| A | HOH683 |
| A | HOH931 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GRG A 503 |
| Chain | Residue |
| A | HIS55 |
| A | ILE206 |
| A | GLY214 |
| A | TYR215 |
| A | ASN294 |
| A | VAL296 |
| A | HIS297 |
| A | TYR340 |
| A | LYS343 |
| A | GRG502 |
| A | GRG504 |
| A | HOH915 |
| A | HOH916 |
| A | HOH940 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GRG A 504 |
| Chain | Residue |
| A | TRP87 |
| A | ASN294 |
| A | HIS297 |
| A | LYS343 |
| A | LEU347 |
| A | PHE350 |
| A | ILE370 |
| A | ILE371 |
| A | ALA379 |
| A | SER380 |
| A | LEU385 |
| A | GRG503 |
| site_id | AC5 |
| Number of Residues | 41 |
| Details | BINDING SITE FOR RESIDUE FDA B 501 |
| Chain | Residue |
| B | THR157 |
| B | GLY158 |
| B | SER160 |
| B | SER162 |
| B | ALA185 |
| B | ALA267 |
| B | GLY287 |
| B | ASP288 |
| B | VAL293 |
| B | GLY298 |
| B | GLY299 |
| B | GLY300 |
| B | LYS301 |
| B | GRG502 |
| B | HOH601 |
| B | HOH604 |
| B | HOH610 |
| B | HOH617 |
| B | HOH618 |
| B | HOH620 |
| B | HOH624 |
| B | HOH646 |
| B | HOH922 |
| B | ILE11 |
| B | GLY12 |
| B | GLY14 |
| B | PHE15 |
| B | ALA16 |
| B | ASP35 |
| B | SER36 |
| B | LYS37 |
| B | LYS45 |
| B | PRO46 |
| B | CYS47 |
| B | GLY48 |
| B | ASP49 |
| B | ALA50 |
| B | THR120 |
| B | THR121 |
| B | ALA122 |
| B | ALA156 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GRG B 502 |
| Chain | Residue |
| B | SER52 |
| B | ASN90 |
| B | GLY91 |
| B | GLU92 |
| B | TYR215 |
| B | TRP217 |
| B | HIS297 |
| B | GLY298 |
| B | GLY299 |
| B | LEU377 |
| B | FDA501 |
| B | GRG503 |
| B | HOH651 |
| B | HOH895 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE GRG B 503 |
| Chain | Residue |
| B | HIS55 |
| B | ILE206 |
| B | GLY214 |
| B | TYR215 |
| B | ASN294 |
| B | VAL296 |
| B | HIS297 |
| B | TYR340 |
| B | LYS343 |
| B | SER380 |
| B | GRG502 |
| B | GRG504 |
| B | HOH704 |
| B | HOH928 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GRG B 504 |
| Chain | Residue |
| B | ASN294 |
| B | HIS297 |
| B | LYS343 |
| B | LEU347 |
| B | PHE350 |
| B | ILE371 |
| B | ALA379 |
| B | SER380 |
| B | LEU409 |
| B | GRG503 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21515284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24954619","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ATQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OPC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24954619","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4OPC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
