1QU4
CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI ORNITHINE DECARBOXYLASE
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 | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004586 | molecular_function | ornithine decarboxylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004586 | molecular_function | ornithine decarboxylase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004586 | molecular_function | ornithine decarboxylase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0033387 | biological_process | putrescine biosynthetic process from ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | ALA67 |
| A | GLY276 |
| A | ARG277 |
| A | TYR389 |
| B | CYS360 |
| A | LYS69 |
| A | ASP88 |
| A | ARG154 |
| A | HIS197 |
| A | SER200 |
| A | GLY236 |
| A | GLY237 |
| A | GLU274 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| A | CYS360 |
| B | ALA67 |
| B | LYS69 |
| B | ASP88 |
| B | ARG154 |
| B | HIS197 |
| B | SER200 |
| B | GLY236 |
| B | GLY237 |
| B | GLU274 |
| B | GLY276 |
| B | ARG277 |
| B | TYR389 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 600 |
| Chain | Residue |
| C | LYS69 |
| C | ASP88 |
| C | ARG154 |
| C | HIS197 |
| C | SER200 |
| C | GLY236 |
| C | GLY237 |
| C | GLU274 |
| C | GLY276 |
| C | ARG277 |
| C | TYR389 |
| D | CYS360 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP D 600 |
| Chain | Residue |
| C | CYS360 |
| D | LYS69 |
| D | ASP88 |
| D | ARG154 |
| D | HIS197 |
| D | SER200 |
| D | GLY236 |
| D | GLY237 |
| D | GLU274 |
| D | GLY276 |
| D | ARG277 |
| D | TYR389 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor; shared with dimeric partner => ECO:0000269|PubMed:10985770, ECO:0000269|PubMed:15476392 |
| Chain | Residue | Details |
| A | CYS360 | |
| B | CYS360 | |
| C | CYS360 | |
| D | CYS360 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10563800, ECO:0000269|PubMed:10985770, ECO:0000269|PubMed:15476392 |
| Chain | Residue | Details |
| A | SER200 | |
| C | SER200 | |
| C | GLY237 | |
| C | GLU274 | |
| C | TYR389 | |
| D | SER200 | |
| D | GLY237 | |
| D | GLU274 | |
| D | TYR389 | |
| A | GLY237 | |
| A | GLU274 | |
| A | TYR389 | |
| B | SER200 | |
| B | GLY237 | |
| B | GLU274 | |
| B | TYR389 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:10563800, ECO:0000269|PubMed:10985770 |
| Chain | Residue | Details |
| A | TYR331 | |
| B | TYR331 | |
| C | TYR331 | |
| D | TYR331 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10563800, ECO:0000269|PubMed:10985770 |
| Chain | Residue | Details |
| A | ASP361 | |
| B | ASP361 | |
| C | ASP361 | |
| D | ASP361 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Stacks against the aromatic ring of pyridoxal phosphate and stabilizes reaction intermediates => ECO:0000305|PubMed:10563800 |
| Chain | Residue | Details |
| A | HIS197 | |
| B | HIS197 | |
| C | HIS197 | |
| D | HIS197 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10563800, ECO:0000269|PubMed:15476392, ECO:0007744|PDB:1QU4 |
| Chain | Residue | Details |
| A | LYS69 | |
| B | LYS69 | |
| C | LYS69 | |
| D | LYS69 |
