3N29
Crystal structure of carboxynorspermidine decarboxylase complexed with Norspermidine from Campylobacter jejuni
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| 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 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045312 | biological_process | nor-spermidine biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0008836 | molecular_function | diaminopimelate decarboxylase activity |
| 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 |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045312 | biological_process | nor-spermidine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | ALA39 |
| A | HOH442 |
| A | HOH459 |
| A | HOH523 |
| A | NSD1002 |
| B | CYS313 |
| B | HOH500 |
| A | LYS41 |
| A | HIS166 |
| A | GLY201 |
| A | GLY202 |
| A | GLU233 |
| A | GLY235 |
| A | GLU236 |
| A | TYR342 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NSD A 1002 |
| Chain | Residue |
| A | CYS169 |
| A | GLU236 |
| A | ASP272 |
| A | MET276 |
| A | TYR342 |
| A | LYS346 |
| A | HOH459 |
| A | PLP1001 |
| B | LEU314 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1003 |
| Chain | Residue |
| A | ASP272 |
| A | TYR278 |
| A | ASP338 |
| A | HIS341 |
| A | TYR342 |
| A | THR343 |
| A | HOH383 |
| A | HOH426 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 1001 |
| Chain | Residue |
| A | CYS313 |
| A | HOH455 |
| B | ALA39 |
| B | LYS41 |
| B | HIS166 |
| B | GLY201 |
| B | GLY202 |
| B | GLU233 |
| B | PRO234 |
| B | GLY235 |
| B | GLU236 |
| B | TYR342 |
| B | HOH402 |
| B | HOH495 |
| B | HOH526 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1003 |
| Chain | Residue |
| B | ASP272 |
| B | TYR278 |
| B | ASP338 |
| B | HIS341 |
| B | TYR342 |
| B | HOH406 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20534592 |
| Chain | Residue | Details |
| A | GLU236 | |
| A | ASP272 | |
| B | GLU236 | |
| B | ASP272 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20534592 |
| Chain | Residue | Details |
| A | LYS41 | |
| B | LYS41 |
