4JZB
Crystal Structure of Leshmaniasis major Farnesyl diphosphate synthase in complex with 1-(2-HYDROXY-2,2-DIPHOSPHONOETHYL)-3-PHENYLPYRIDINIUM, IPP and Ca2+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004161 | molecular_function | dimethylallyltranstransferase activity |
A | 0004337 | molecular_function | geranyltranstransferase activity |
A | 0004659 | molecular_function | prenyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0004161 | molecular_function | dimethylallyltranstransferase activity |
B | 0004337 | molecular_function | geranyltranstransferase activity |
B | 0004659 | molecular_function | prenyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008299 | biological_process | isoprenoid biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
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 CA A 401 |
Chain | Residue |
A | ASP98 |
A | ASP102 |
A | CA402 |
A | P2H405 |
A | HOH502 |
A | HOH503 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 402 |
Chain | Residue |
A | P2H405 |
A | HOH501 |
A | HOH504 |
A | HOH511 |
A | ASP98 |
A | ASP102 |
A | CA401 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | ASP250 |
A | P2H405 |
A | HOH505 |
A | HOH506 |
A | HOH512 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE IPE A 404 |
Chain | Residue |
A | GLY47 |
A | LYS48 |
A | ARG51 |
A | GLN91 |
A | ARG108 |
A | THR208 |
A | TYR211 |
A | PHE246 |
A | GLN247 |
A | ASP250 |
A | P2H405 |
A | HOH509 |
A | HOH531 |
A | HOH536 |
A | HOH552 |
A | HOH587 |
A | HOH617 |
A | HOH645 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE P2H A 405 |
Chain | Residue |
A | PHE94 |
A | ASP98 |
A | MET101 |
A | ASP102 |
A | ARG107 |
A | THR163 |
A | GLN167 |
A | LYS207 |
A | THR208 |
A | ASP250 |
A | LYS264 |
A | CA401 |
A | CA402 |
A | CA403 |
A | IPE404 |
A | HOH504 |
A | HOH513 |
A | HOH532 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 406 |
Chain | Residue |
A | GLY266 |
A | GLU270 |
A | HOH554 |
A | HOH561 |
A | HOH671 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE IPE B 401 |
Chain | Residue |
B | GLY47 |
B | LYS48 |
B | ARG51 |
B | GLN91 |
B | ARG108 |
B | THR208 |
B | TYR211 |
B | PHE246 |
B | GLN247 |
B | ASP250 |
B | P2H402 |
B | HOH509 |
B | HOH523 |
B | HOH527 |
B | HOH542 |
B | HOH580 |
B | HOH622 |
B | HOH651 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE P2H B 402 |
Chain | Residue |
B | PHE94 |
B | ASP98 |
B | MET101 |
B | ASP102 |
B | ARG107 |
B | THR163 |
B | GLN167 |
B | LYS207 |
B | THR208 |
B | ASP250 |
B | LYS264 |
B | IPE401 |
B | CA403 |
B | CA404 |
B | CA405 |
B | HOH504 |
B | HOH513 |
B | HOH545 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 403 |
Chain | Residue |
B | HOH503 |
B | HOH511 |
B | ASP98 |
B | ASP102 |
B | P2H402 |
B | CA405 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 404 |
Chain | Residue |
B | ASP250 |
B | P2H402 |
B | HOH505 |
B | HOH506 |
B | HOH514 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 405 |
Chain | Residue |
B | ASP98 |
B | ASP102 |
B | P2H402 |
B | CA403 |
B | HOH502 |
B | HOH504 |
B | HOH512 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 406 |
Chain | Residue |
B | GLY266 |
B | GLU270 |
B | HOH562 |
B | HOH615 |
B | HOH766 |
Functional Information from PROSITE/UniProt