1NJJ
Crystal structure determination of T. brucei ornithine decarboxylase bound to D-ornithine and to G418
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004586 | molecular_function | ornithine decarboxylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006595 | biological_process | polyamine metabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0033387 | biological_process | putrescine biosynthetic process from arginine, via ornithine |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004586 | molecular_function | ornithine decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006595 | biological_process | polyamine metabolic process |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0033387 | biological_process | putrescine biosynthetic process from arginine, via ornithine |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004586 | molecular_function | ornithine decarboxylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006595 | biological_process | polyamine metabolic process |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0033387 | biological_process | putrescine biosynthetic process from arginine, via ornithine |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004586 | molecular_function | ornithine decarboxylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006595 | biological_process | polyamine metabolic process |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0033387 | biological_process | putrescine biosynthetic process from arginine, via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GET A 601 |
| Chain | Residue |
| A | ARG22 |
| A | ASP243 |
| A | LEU339 |
| A | PRO340 |
| A | GLN341 |
| A | LEU382 |
| A | GLU384 |
| A | ASP385 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GET B 602 |
| Chain | Residue |
| B | CYS26 |
| B | ASP243 |
| B | PRO340 |
| B | GLN341 |
| B | ARG342 |
| B | GLU343 |
| B | LEU382 |
| B | GLU384 |
| B | ASP385 |
| B | HOH629 |
| B | HOH631 |
| B | ARG22 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GET C 603 |
| Chain | Residue |
| C | ARG22 |
| C | ASP243 |
| C | PRO340 |
| C | GLN341 |
| C | GLU343 |
| C | LEU382 |
| C | GLU384 |
| C | ASP385 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ORX A 602 |
| Chain | Residue |
| A | LYS69 |
| A | ASP88 |
| A | HIS197 |
| A | GLY236 |
| A | GLY237 |
| A | GLU274 |
| A | GLY276 |
| A | ARG277 |
| A | TYR331 |
| A | ASP332 |
| A | TYR389 |
| A | HOH610 |
| A | HOH632 |
| B | TYR323 |
| B | CYS360 |
| B | ASP361 |
| B | GLY362 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ORX B 603 |
| Chain | Residue |
| A | TYR323 |
| A | CYS360 |
| A | ASP361 |
| B | LYS69 |
| B | ASP88 |
| B | ARG154 |
| B | HIS197 |
| B | GLY236 |
| B | GLY237 |
| B | GLU274 |
| B | GLY276 |
| B | ARG277 |
| B | TYR331 |
| B | ASP332 |
| B | TYR389 |
| B | HOH604 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ORX C 604 |
| Chain | Residue |
| C | LYS69 |
| C | ASP88 |
| C | ARG154 |
| C | HIS197 |
| C | GLY236 |
| C | GLY237 |
| C | GLU274 |
| C | GLY276 |
| C | ARG277 |
| C | TYR331 |
| C | ASP332 |
| C | TYR389 |
| C | HOH634 |
| C | HOH652 |
| D | TYR323 |
| D | CYS360 |
| D | ASP361 |
| D | HOH467 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ORX D 426 |
| Chain | Residue |
| C | CYS360 |
| C | ASP361 |
| C | GLY362 |
| D | LYS69 |
| D | ASP88 |
| D | HIS197 |
| D | GLY237 |
| D | GLU274 |
| D | PRO275 |
| D | GLY276 |
| D | ARG277 |
| D | TYR331 |
| D | ASP332 |
| D | TYR389 |
| D | HOH434 |
| D | HOH438 |
| D | HOH442 |
Functional Information from PROSITE/UniProt
| site_id | PS00878 |
| Number of Residues | 19 |
| Details | ODR_DC_2_1 Orn/DAP/Arg decarboxylases family 2 pyridoxal-P attachment site. YAvKCNddwrVLgtLaalG |
| Chain | Residue | Details |
| A | TYR66-GLY84 |
| site_id | PS00879 |
| Number of Residues | 18 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. GtelgfnMhILDIGGGFP |
| Chain | Residue | Details |
| A | GLY222-PRO239 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | LYS169 | |
| A | LYS69 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | LYS169 | |
| B | LYS69 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| C | LYS169 | |
| C | LYS69 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| D | LYS169 | |
| D | LYS69 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | GLU274 | |
| A | LYS69 | |
| A | HIS197 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | GLU274 | |
| B | LYS69 | |
| B | HIS197 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| C | GLU274 | |
| C | LYS69 | |
| C | HIS197 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| D | GLU274 | |
| D | LYS69 | |
| D | HIS197 |
