3N2B
1.8 Angstrom Resolution Crystal Structure of Diaminopimelate Decarboxylase (lysA) from Vibrio cholerae.
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| C | 0009085 | biological_process | lysine biosynthetic process |
| C | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| D | 0009085 | biological_process | lysine biosynthetic process |
| D | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 418 |
| Chain | Residue |
| A | GLU128 |
| A | ARG178 |
| B | LYS295 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 418 |
| Chain | Residue |
| C | PRO276 |
| C | GLY277 |
| C | ARG278 |
| C | ALA279 |
| C | HOH992 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 419 |
| Chain | Residue |
| C | PRO161 |
| C | TYR162 |
| C | ILE163 |
| C | HOH619 |
| C | HIS160 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL D 418 |
| Chain | Residue |
| D | GLY240 |
| D | PRO276 |
| D | GLY277 |
| D | ARG278 |
| D | ALA279 |
| D | HOH1079 |
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. YAvKANsnlgVLntLarlG |
| Chain | Residue | Details |
| A | TYR58-GLY76 |
| site_id | PS00879 |
| Number of Residues | 16 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. Aegih..IrHLDVGGGLG |
| Chain | Residue | Details |
| A | ALA227-GLY242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255 |
| Chain | Residue | Details |
| A | CYS344 | |
| B | CYS344 | |
| C | CYS344 | |
| D | CYS344 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY240 | |
| B | ARG278 | |
| B | ARG314 | |
| B | TYR318 | |
| B | GLU345 | |
| B | TYR372 | |
| C | GLY240 | |
| C | GLU275 | |
| C | ARG278 | |
| C | ARG314 | |
| C | TYR318 | |
| A | GLU275 | |
| C | GLU345 | |
| C | TYR372 | |
| D | GLY240 | |
| D | GLU275 | |
| D | ARG278 | |
| D | ARG314 | |
| D | TYR318 | |
| D | GLU345 | |
| D | TYR372 | |
| A | ARG278 | |
| A | ARG314 | |
| A | TYR318 | |
| A | GLU345 | |
| A | TYR372 | |
| B | GLY240 | |
| B | GLU275 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS61 | |
| B | LYS61 | |
| C | LYS61 | |
| D | LYS61 |
