2P3E
Crystal structure of AQ1208 from Aquifex aeolicus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| A | 0009085 | biological_process | lysine biosynthetic process |
| A | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| B | 0009085 | biological_process | lysine biosynthetic process |
| B | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
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. YAvKANfnphLVklLgelG |
| Chain | Residue | Details |
| A | TYR62-GLY80 |
| site_id | PS00879 |
| Number of Residues | 14 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Gfd....IkYLDIGGGLG |
| Chain | Residue | Details |
| A | GLY233-GLY246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255 |
| Chain | Residue | Details |
| A | CYS348 | |
| B | CYS348 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY244 | |
| B | ARG282 | |
| B | ARG318 | |
| B | TYR322 | |
| B | GLU349 | |
| B | TYR377 | |
| A | GLU279 | |
| A | ARG282 | |
| A | ARG318 | |
| A | TYR322 | |
| A | GLU349 | |
| A | TYR377 | |
| B | GLY244 | |
| B | GLU279 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS65 | |
| B | LYS65 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | LYS175 | |
| A | LYS65 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | LYS175 | |
| B | LYS65 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | GLU279 | |
| A | LYS65 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| B | HIS204 | |
| B | GLU279 | |
| B | LYS65 |
