4JZX
Crystal Structure of Leshmaniasis major Farnesyl diphosphate synthase in complex with 3-BUTYL-1-(2,2-DIPHOSPHONOETHYL)PYRIDINIUM, 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 | 18 |
Details | BINDING SITE FOR RESIDUE IPE A 401 |
Chain | Residue |
A | GLY47 |
A | ASP250 |
A | 476402 |
A | HOH509 |
A | HOH513 |
A | HOH533 |
A | HOH551 |
A | HOH553 |
A | HOH573 |
A | HOH597 |
A | LYS48 |
A | ARG51 |
A | GLN91 |
A | ARG108 |
A | THR208 |
A | TYR211 |
A | PHE246 |
A | GLN247 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 476 A 402 |
Chain | Residue |
A | PHE94 |
A | ASP98 |
A | ASP102 |
A | ARG107 |
A | THR163 |
A | GLN167 |
A | LYS207 |
A | THR208 |
A | ASP250 |
A | LYS264 |
A | IPE401 |
A | CA403 |
A | CA404 |
A | CA405 |
A | HOH504 |
A | HOH534 |
A | HOH562 |
B | ASN126 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 403 |
Chain | Residue |
A | ASP98 |
A | ASP102 |
A | 476402 |
A | CA405 |
A | HOH501 |
A | HOH504 |
A | HOH543 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 404 |
Chain | Residue |
A | ASP250 |
A | 476402 |
A | HOH505 |
A | HOH506 |
A | HOH545 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 405 |
Chain | Residue |
A | ASP98 |
A | ASP102 |
A | 476402 |
A | CA403 |
A | HOH502 |
A | HOH503 |
site_id | AC6 |
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 | 476402 |
B | HOH509 |
B | HOH512 |
B | HOH528 |
B | HOH539 |
B | HOH560 |
B | HOH563 |
B | HOH584 |
site_id | AC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 476 B 402 |
Chain | Residue |
A | ASN126 |
B | PHE94 |
B | ASP98 |
B | ASP102 |
B | ARG107 |
B | GLN167 |
B | LYS207 |
B | THR208 |
B | ASP250 |
B | LYS264 |
B | IPE401 |
B | CA403 |
B | CA404 |
B | CA405 |
B | HOH504 |
B | HOH595 |
B | HOH608 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 403 |
Chain | Residue |
B | ASP98 |
B | ASP102 |
B | 476402 |
B | CA405 |
B | HOH502 |
B | HOH504 |
B | HOH527 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 404 |
Chain | Residue |
B | HOH506 |
B | HOH525 |
B | ASP250 |
B | 476402 |
B | HOH505 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 405 |
Chain | Residue |
B | ASP98 |
B | ASP102 |
B | 476402 |
B | CA403 |
B | HOH503 |
B | HOH790 |
Functional Information from PROSITE/UniProt