2TOD
ORNITHINE DECARBOXYLASE FROM TRYPANOSOMA BRUCEI K69A MUTANT IN COMPLEX WITH ALPHA-DIFLUOROMETHYLORNITHINE
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 | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 600 |
| Chain | Residue |
| A | CYS360 |
| A | DMO700 |
| B | ALA67 |
| B | ARG154 |
| B | HIS197 |
| B | SER200 |
| B | GLY236 |
| B | GLY237 |
| B | GLU274 |
| B | GLY276 |
| B | ARG277 |
| B | TYR389 |
| B | HOH708 |
| B | HOH741 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMO A 700 |
| Chain | Residue |
| A | CYS360 |
| A | ASP361 |
| A | PHE397 |
| A | HOH728 |
| B | TYR331 |
| B | ASP332 |
| B | PLP600 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 600 |
| Chain | Residue |
| A | ASP88 |
| A | ARG154 |
| A | HIS197 |
| A | SER200 |
| A | GLY236 |
| A | GLY237 |
| A | GLU274 |
| A | GLY276 |
| A | ARG277 |
| A | TYR389 |
| A | HOH719 |
| A | HOH768 |
| B | CYS360 |
| B | DMO700 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMO B 700 |
| Chain | Residue |
| A | TYR331 |
| A | ASP332 |
| A | PLP600 |
| B | CYS360 |
| B | ASP361 |
| B | PHE397 |
| B | HOH707 |
| B | HOH757 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP D 600 |
| Chain | Residue |
| C | CYS360 |
| C | DMO700 |
| D | ALA67 |
| D | ARG154 |
| D | HIS197 |
| D | SER200 |
| D | GLY236 |
| D | GLY237 |
| D | GLU274 |
| D | PRO275 |
| D | GLY276 |
| D | ARG277 |
| D | TYR389 |
| D | HOH715 |
| D | HOH730 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMO C 700 |
| Chain | Residue |
| C | CYS360 |
| C | ASP361 |
| C | PHE397 |
| C | HOH714 |
| C | HOH773 |
| D | TYR331 |
| D | ASP332 |
| D | PLP600 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP C 600 |
| Chain | Residue |
| C | ALA67 |
| C | ASP88 |
| C | ARG154 |
| C | HIS197 |
| C | SER200 |
| C | GLY236 |
| C | GLY237 |
| C | GLU274 |
| C | GLY276 |
| C | ARG277 |
| C | TYR389 |
| C | HOH711 |
| C | HOH752 |
| C | HOH813 |
| D | CYS360 |
| D | DMO700 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMO D 700 |
| Chain | Residue |
| C | TYR331 |
| C | ASP332 |
| C | PLP600 |
| D | CYS360 |
| D | ASP361 |
| D | PHE397 |
| D | HOH708 |
| D | HOH725 |
| site_id | CAA |
| Number of Residues | 14 |
| Details | CATALYTIC SITE |
| Chain | Residue |
| A | ALA69 |
| A | ASP332 |
| A | TYR331 |
| A | TYR323 |
| A | PHE397 |
| A | ASP361 |
| A | ARG154 |
| A | GLU274 |
| A | HIS197 |
| A | GLY237 |
| A | SER200 |
| A | ARG277 |
| A | CYS360 |
| A | TYR389 |
| site_id | CAB |
| Number of Residues | 14 |
| Details | CATALYTIC SITE |
| Chain | Residue |
| B | ALA69 |
| B | ARG154 |
| B | GLU274 |
| B | HIS197 |
| B | GLY237 |
| B | SER200 |
| B | ARG277 |
| B | CYS360 |
| B | TYR389 |
| B | ASP332 |
| B | TYR331 |
| B | TYR323 |
| B | PHE397 |
| B | ASP361 |
| site_id | CAC |
| Number of Residues | 14 |
| Details | CATALYTIC SITE |
| Chain | Residue |
| C | ALA69 |
| C | ARG154 |
| C | GLU274 |
| C | HIS197 |
| C | GLY237 |
| C | SER200 |
| C | ARG277 |
| C | CYS360 |
| C | TYR389 |
| C | ASP332 |
| C | TYR331 |
| C | TYR323 |
| C | PHE397 |
| C | ASP361 |
| site_id | CAD |
| Number of Residues | 14 |
| Details | CATALYTIC SITE |
| Chain | Residue |
| D | ALA69 |
| D | ARG154 |
| D | GLU274 |
| D | HIS197 |
| D | GLY237 |
| D | SER200 |
| D | ARG277 |
| D | CYS360 |
| D | TYR389 |
| D | ASP332 |
| D | TYR331 |
| D | TYR323 |
| D | PHE397 |
| D | ASP361 |
Functional Information from PROSITE/UniProt
| 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 | 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 | |
| C | SER200 |
| 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 | ALA69 | |
| B | ALA69 | |
| C | ALA69 | |
| D | ALA69 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 7odc |
| Chain | Residue | Details |
| A | GLU274 | |
| A | ALA69 | |
| A | HIS197 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 7odc |
| Chain | Residue | Details |
| B | GLU274 | |
| B | ALA69 | |
| B | HIS197 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 7odc |
| Chain | Residue | Details |
| C | GLU274 | |
| C | ALA69 | |
| C | HIS197 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 7odc |
| Chain | Residue | Details |
| D | GLU274 | |
| D | ALA69 | |
| D | HIS197 |
