5XK7
Crystal structure of Isosesquilavandulyl Diphosphate Synthase from Streptomyces sp. strain CNH-189 in complex with DMAPP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002094 | molecular_function | polyprenyltransferase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0009409 | biological_process | response to cold |
A | 0009668 | biological_process | plastid membrane organization |
A | 0016094 | biological_process | polyprenol biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0033850 | molecular_function | Z-farnesyl diphosphate synthase activity |
A | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0002094 | molecular_function | polyprenyltransferase activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0009409 | biological_process | response to cold |
B | 0009668 | biological_process | plastid membrane organization |
B | 0016094 | biological_process | polyprenol biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0033850 | molecular_function | Z-farnesyl diphosphate synthase activity |
B | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0002094 | molecular_function | polyprenyltransferase activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0009409 | biological_process | response to cold |
C | 0009668 | biological_process | plastid membrane organization |
C | 0016094 | biological_process | polyprenol biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
C | 0033850 | molecular_function | Z-farnesyl diphosphate synthase activity |
C | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0002094 | molecular_function | polyprenyltransferase activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0009409 | biological_process | response to cold |
D | 0009668 | biological_process | plastid membrane organization |
D | 0016094 | biological_process | polyprenol biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
D | 0033850 | molecular_function | Z-farnesyl diphosphate synthase activity |
D | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue MG A 301 |
Chain | Residue |
A | ASP9 |
A | POP302 |
A | POP303 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue POP A 302 |
Chain | Residue |
A | ARG60 |
A | MG301 |
A | POP303 |
A | HOH512 |
A | ASP9 |
A | GLY10 |
A | MET11 |
A | ARG12 |
A | ARG13 |
A | TYR26 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue POP A 303 |
Chain | Residue |
A | ASP9 |
A | SER54 |
A | ASN57 |
A | ARG60 |
A | ARG163 |
A | ARG169 |
A | SER171 |
A | PHE173 |
A | MG301 |
A | POP302 |
A | HOH404 |
A | HOH405 |
A | HOH413 |
A | HOH448 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue MES A 304 |
Chain | Residue |
A | TYR184 |
A | PHE185 |
A | ASP204 |
A | ARG208 |
A | HOH436 |
A | HOH484 |
A | HOH530 |
B | VAL168 |
B | HOH458 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 305 |
Chain | Residue |
A | ARG211 |
A | HOH406 |
A | HOH491 |
B | ARG13 |
B | HIS167 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue MG B 301 |
Chain | Residue |
B | ASP9 |
B | POP302 |
B | DMA303 |
B | HOH411 |
B | HOH489 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue POP B 302 |
Chain | Residue |
A | TYR215 |
B | ASP9 |
B | GLY10 |
B | MET11 |
B | ARG12 |
B | ARG13 |
B | TYR26 |
B | ARG60 |
B | MG301 |
B | DMA303 |
B | HOH411 |
B | HOH429 |
B | HOH489 |
site_id | AC8 |
Number of Residues | 23 |
Details | binding site for residue DMA B 303 |
Chain | Residue |
A | PHE180 |
A | ARG211 |
A | TYR212 |
A | GLY213 |
B | LEU7 |
B | PRO8 |
B | ASP9 |
B | THR51 |
B | VAL52 |
B | ASN57 |
B | ARG60 |
B | ARG163 |
B | ARG169 |
B | SER171 |
B | PHE173 |
B | MG301 |
B | POP302 |
B | HOH411 |
B | HOH427 |
B | HOH429 |
B | HOH445 |
B | HOH454 |
B | HOH489 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MES B 304 |
Chain | Residue |
A | VAL168 |
B | TYR184 |
B | PHE185 |
B | CYS186 |
B | PRO187 |
B | ARG208 |
B | HOH458 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG C 301 |
Chain | Residue |
C | ASP9 |
C | POP302 |
C | DMA303 |
C | HOH513 |
C | HOH528 |
site_id | AD2 |
Number of Residues | 12 |
Details | binding site for residue POP C 302 |
Chain | Residue |
C | TYR26 |
C | ARG60 |
C | MG301 |
C | DMA303 |
C | HOH470 |
C | HOH513 |
C | HOH528 |
C | ASP9 |
C | GLY10 |
C | MET11 |
C | ARG12 |
C | ARG13 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue DMA C 303 |
Chain | Residue |
C | LEU7 |
C | PRO8 |
C | THR51 |
C | VAL52 |
C | ASN57 |
C | ARG163 |
C | ARG169 |
C | SER171 |
C | PHE173 |
C | MG301 |
C | POP302 |
C | HOH407 |
C | HOH459 |
C | HOH528 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue MES C 304 |
Chain | Residue |
C | TYR184 |
C | PHE185 |
C | CYS186 |
C | ARG208 |
D | HOH536 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue SO4 C 305 |
Chain | Residue |
C | ARG211 |
C | HOH403 |
C | HOH411 |
C | HOH523 |
D | ARG13 |
D | HIS167 |
D | HOH490 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue MG D 301 |
Chain | Residue |
D | ASP9 |
D | POP302 |
D | DMA303 |
D | HOH405 |
D | HOH432 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue POP D 302 |
Chain | Residue |
C | ARG211 |
C | TYR215 |
D | ASP9 |
D | GLY10 |
D | MET11 |
D | ARG12 |
D | ARG13 |
D | TYR26 |
D | ARG60 |
D | MG301 |
D | DMA303 |
D | HOH405 |
D | HOH432 |
D | HOH471 |
site_id | AD8 |
Number of Residues | 23 |
Details | binding site for residue DMA D 303 |
Chain | Residue |
C | PHE180 |
C | ARG211 |
C | TYR212 |
C | GLY213 |
C | HOH442 |
D | LEU7 |
D | PRO8 |
D | ASP9 |
D | THR51 |
D | VAL52 |
D | ASN57 |
D | ARG60 |
D | ARG163 |
D | ARG169 |
D | SER171 |
D | PHE173 |
D | MG301 |
D | POP302 |
D | HOH405 |
D | HOH422 |
D | HOH423 |
D | HOH432 |
D | HOH471 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue MES D 304 |
Chain | Residue |
C | VAL168 |
D | TYR184 |
D | PHE185 |
D | PRO187 |
D | ARG208 |
D | HOH446 |
D | HOH536 |