4LFE
Crystal structure of geranylgeranyl diphosphate synthase sub1274 (target efi-509455) from streptococcus uberis 0140j with bound magnesium and isopentyl diphosphate, partially liganded complex;
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004337 | molecular_function | (2E,6E)-farnesyl diphosphate synthase activity |
A | 0004659 | molecular_function | prenyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0016114 | biological_process | terpenoid biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004337 | molecular_function | (2E,6E)-farnesyl diphosphate synthase activity |
B | 0004659 | molecular_function | prenyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008299 | biological_process | isoprenoid biosynthetic process |
B | 0016114 | biological_process | terpenoid biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE IPE A 301 |
Chain | Residue |
A | SER74 |
A | HOH415 |
A | HOH417 |
A | HOH419 |
A | HOH452 |
A | HOH454 |
A | HOH467 |
A | HOH489 |
A | LEU75 |
A | ASP78 |
A | ASP84 |
A | ARG89 |
A | LYS172 |
A | MG302 |
A | MG303 |
A | HOH403 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 302 |
Chain | Residue |
A | ASP78 |
A | ASP84 |
A | IPE301 |
A | MG303 |
A | HOH436 |
A | HOH454 |
A | HOH471 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 303 |
Chain | Residue |
A | ASP78 |
A | ASP84 |
A | IPE301 |
A | MG302 |
A | HOH419 |
A | HOH452 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE IPE B 301 |
Chain | Residue |
B | ASP78 |
B | ASP84 |
B | ARG89 |
B | LYS172 |
B | THR173 |
B | GLN210 |
B | ASP213 |
B | LYS227 |
B | IPE302 |
B | MG303 |
B | MG304 |
B | MG305 |
B | HOH409 |
B | HOH420 |
B | HOH431 |
B | HOH436 |
B | HOH474 |
B | HOH484 |
B | HOH496 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE IPE B 302 |
Chain | Residue |
B | GLY37 |
B | LYS38 |
B | ARG41 |
B | HIS71 |
B | LEU75 |
B | ARG90 |
B | THR173 |
B | PHE209 |
B | GLN210 |
B | ASP213 |
B | IPE301 |
B | HOH402 |
B | HOH404 |
B | HOH406 |
B | HOH423 |
B | HOH430 |
B | HOH518 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 303 |
Chain | Residue |
B | ASP213 |
B | IPE301 |
B | HOH416 |
B | HOH420 |
B | HOH436 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 304 |
Chain | Residue |
B | ASP78 |
B | ASP84 |
B | IPE301 |
B | MG305 |
B | HOH419 |
B | HOH458 |
B | HOH496 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 305 |
Chain | Residue |
B | ASP78 |
B | ASP84 |
B | IPE301 |
B | MG304 |
B | HOH431 |
B | HOH474 |
Functional Information from PROSITE/UniProt