3M9U
Crystal structure of geranylgeranyl pyrophosphate synthase from lactobacillus brevis atcc 367
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
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 | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0004337 | molecular_function | geranyltranstransferase activity |
C | 0004659 | molecular_function | prenyltransferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0008299 | biological_process | isoprenoid biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0004337 | molecular_function | geranyltranstransferase activity |
D | 0004659 | molecular_function | prenyltransferase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0008299 | biological_process | isoprenoid biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 309 |
Chain | Residue |
A | LEU275 |
A | LEU278 |
A | PRO279 |
A | THR280 |
A | SER281 |
A | ARG284 |
A | ASP285 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 310 |
Chain | Residue |
A | ASP90 |
A | THR105 |
A | ASN106 |
A | SER42 |
A | ALA45 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 311 |
Chain | Residue |
A | ARG70 |
A | HIS71 |
A | MET139 |
A | LEU198 |
A | HOH757 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 312 |
Chain | Residue |
A | ASP266 |
A | SER270 |
A | HOH343 |
A | HOH402 |
D | SER61 |
D | SER281 |
D | GLN283 |
D | ARG284 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 313 |
Chain | Residue |
A | THR131 |
A | ALA132 |
A | THR133 |
A | ASP134 |
A | GLN140 |
A | ASN170 |
A | PRO172 |
A | HOH409 |
A | HOH474 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 314 |
Chain | Residue |
A | VAL67 |
A | LEU255 |
A | GLY256 |
A | LEU257 |
A | ILE258 |
A | GLY259 |
A | HOH454 |
A | HOH515 |
A | HOH843 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 309 |
Chain | Residue |
B | ARG6 |
B | PHE10 |
B | ALA57 |
B | ASP286 |
B | HOH362 |
B | HOH529 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 310 |
Chain | Residue |
B | SER42 |
B | ASP90 |
B | ARG100 |
B | THR105 |
B | ASN106 |
B | HOH429 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 309 |
Chain | Residue |
C | PRO21 |
C | PRO68 |
C | ARG73 |
C | GLN175 |
C | HOH353 |
C | HOH372 |
C | HOH526 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 310 |
Chain | Residue |
C | ASN19 |
C | ALA20 |
C | LEU22 |
C | LYS23 |
C | HOH338 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 311 |
Chain | Residue |
C | SER42 |
C | ALA45 |
C | ILE87 |
C | ASP90 |
C | THR105 |
C | ASN106 |
C | HOH349 |
C | HOH542 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 312 |
Chain | Residue |
C | LEU86 |
C | ASP89 |
C | GLN160 |
C | LYS183 |
C | HOH457 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 313 |
Chain | Residue |
C | GLN13 |
C | TRP14 |
C | PRO68 |
C | PRO172 |
C | HOH569 |
C | HOH847 |
C | HOH848 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 314 |
Chain | Residue |
C | ARG6 |
C | PHE10 |
C | ALA57 |
C | ASP286 |
C | ALA289 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 309 |
Chain | Residue |
D | HIS82 |
D | LEU86 |
D | ASP89 |
D | GLN160 |
D | LYS183 |
D | THR184 |
D | HOH764 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 310 |
Chain | Residue |
D | ARG70 |
D | HIS71 |
D | LEU198 |
D | HOH678 |
D | HOH840 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 311 |
Chain | Residue |
D | GLY47 |
D | LYS48 |
D | HIS82 |
D | LEU86 |
D | ARG101 |
D | HOH341 |
D | HOH390 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 312 |
Chain | Residue |
D | ASP163 |
D | LEU179 |
D | ASN249 |
D | HOH322 |
D | HOH342 |
D | HOH676 |
site_id | CC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 313 |
Chain | Residue |
A | SER61 |
A | LEU62 |
A | GLY63 |
A | SER281 |
A | GLN283 |
A | ARG284 |
D | ASP266 |
D | HOH402 |
D | HOH415 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 314 |
Chain | Residue |
D | SER42 |
D | ASP90 |
D | ARG100 |
D | THR105 |
D | ASN106 |
D | HOH440 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 315 |
Chain | Residue |
D | LEU275 |
D | LEU278 |
D | PRO279 |
D | THR280 |
D | SER281 |
D | ARG284 |
D | ASP285 |
D | HOH651 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 316 |
Chain | Residue |
D | PRO21 |
D | GLN24 |
D | ARG73 |
Functional Information from PROSITE/UniProt