6W3Z
Crystal Structure of Brugia malayi Deoxyhypusine synthase (DHPS)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
| A | 0016740 | molecular_function | transferase activity |
| A | 0034038 | molecular_function | deoxyhypusine synthase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
| B | 0016740 | molecular_function | transferase activity |
| B | 0034038 | molecular_function | deoxyhypusine synthase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
| C | 0016740 | molecular_function | transferase activity |
| C | 0034038 | molecular_function | deoxyhypusine synthase activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008612 | biological_process | peptidyl-lysine modification to peptidyl-hypusine |
| D | 0016740 | molecular_function | transferase activity |
| D | 0034038 | molecular_function | deoxyhypusine synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | THR102 |
| A | GLY281 |
| A | ASN305 |
| A | THR306 |
| A | GLY307 |
| A | ALA339 |
| A | ASP340 |
| A | ALA341 |
| A | HOH501 |
| A | HOH540 |
| D | HIS286 |
| A | SER103 |
| D | ASP311 |
| D | SER313 |
| D | ASP314 |
| D | SER315 |
| A | ASN104 |
| A | LEU105 |
| A | SER129 |
| A | ALA130 |
| A | GLY131 |
| A | ASP236 |
| A | GLY280 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ARG111 |
| A | LYS139 |
| A | PRO143 |
| A | HOH536 |
| A | HOH538 |
| A | HOH552 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | THR102 |
| B | SER103 |
| B | ASN104 |
| B | LEU105 |
| B | SER129 |
| B | ALA130 |
| B | GLY131 |
| B | GLU134 |
| B | ASP236 |
| B | GLY280 |
| B | GLY281 |
| B | ASN305 |
| B | THR306 |
| B | GLY307 |
| B | ALA339 |
| B | ASP340 |
| B | ALA341 |
| B | HOH506 |
| B | HOH536 |
| B | HOH568 |
| C | GLY282 |
| C | VAL283 |
| C | HIS286 |
| C | ASP311 |
| C | SER313 |
| C | ASP314 |
| C | SER315 |
| C | NAD401 |
| C | HOH547 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | TYR116 |
| B | VAL357 |
| B | GLN358 |
| D | PHE37 |
| D | ASN38 |
| D | GLY40 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| B | GLY282 |
| B | VAL283 |
| B | HIS286 |
| B | ASP311 |
| B | SER313 |
| B | ASP314 |
| B | SER315 |
| B | NAD401 |
| C | THR102 |
| C | SER103 |
| C | ASN104 |
| C | LEU105 |
| C | SER129 |
| C | ALA130 |
| C | GLY131 |
| C | GLU135 |
| C | ASP236 |
| C | GLY280 |
| C | GLY281 |
| C | VAL304 |
| C | ASN305 |
| C | THR306 |
| C | GLY307 |
| C | ALA339 |
| C | ASP340 |
| C | ALA341 |
| C | HOH512 |
| C | HOH515 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | HOH585 |
| A | ILE32 |
| C | ARG111 |
| C | GLU112 |
| C | LYS139 |
| C | PRO143 |
| C | HOH555 |
| C | HOH571 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL D 401 |
| Chain | Residue |
| D | GLU15 |
| D | MET16 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| B | ILE32 |
| B | HOH519 |
| D | ARG111 |
| D | LYS139 |
| D | PRO143 |
| D | ARG216 |
| D | HOH524 |
| D | HOH530 |
