5GJO
Crystal structure of SrLDC mutant (A225C/T302C) in complex with PLP
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 | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0008923 | molecular_function | lysine decarboxylase activity |
| A | 0009446 | biological_process | putrescine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033387 | biological_process | putrescine biosynthetic process from arginine, via 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 | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0008923 | molecular_function | lysine decarboxylase activity |
| B | 0009446 | biological_process | putrescine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033387 | biological_process | putrescine biosynthetic process from arginine, via ornithine |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | LYS143 |
| A | SER186 |
| A | THR187 |
| A | ALA188 |
| A | HOH613 |
| B | ARG245 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| B | LYS275 |
| B | ARG277 |
| A | THR150 |
| A | GLY153 |
| A | HOH639 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | ARG5 |
| A | HIS306 |
| A | HOH602 |
| A | HOH658 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 404 |
| Chain | Residue |
| A | SER7 |
| A | GLU8 |
| A | HOH512 |
| A | HOH641 |
| A | HOH744 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | THR358 |
| A | ARG359 |
| A | PHE360 |
| A | HOH569 |
| A | HOH652 |
| A | HOH764 |
| B | SER354 |
| B | VAL355 |
| B | ALA357 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue PLP A 406 |
| Chain | Residue |
| A | ALA49 |
| A | LYS51 |
| A | ASP70 |
| A | HIS179 |
| A | SER182 |
| A | GLY218 |
| A | GLY219 |
| A | GLU255 |
| A | GLY257 |
| A | ARG258 |
| A | TYR352 |
| A | HOH516 |
| A | HOH520 |
| A | HOH556 |
| B | CYS323 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 407 |
| Chain | Residue |
| A | GLU157 |
| A | ARG199 |
| A | HOH515 |
| B | ARG199 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 408 |
| Chain | Residue |
| A | TYR298 |
| B | SER294 |
| B | SER356 |
| B | THR358 |
| B | NA405 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 409 |
| Chain | Residue |
| A | ARG199 |
| A | ASP202 |
| B | ARG140 |
| B | GLU192 |
| B | HOH733 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | ARG245 |
| B | LYS143 |
| B | SER186 |
| B | THR187 |
| B | ALA188 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | SER7 |
| B | GLU8 |
| B | HOH528 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 403 |
| Chain | Residue |
| A | SER354 |
| A | VAL355 |
| A | ALA357 |
| A | HOH569 |
| B | THR358 |
| B | ARG359 |
| B | PHE360 |
| B | HOH576 |
| B | HOH688 |
| site_id | AD4 |
| Number of Residues | 16 |
| Details | binding site for residue PLP B 404 |
| Chain | Residue |
| A | CYS323 |
| B | ALA49 |
| B | LYS51 |
| B | ASP70 |
| B | ALA93 |
| B | HIS179 |
| B | SER182 |
| B | GLY218 |
| B | GLY219 |
| B | GLU255 |
| B | GLY257 |
| B | ARG258 |
| B | TYR352 |
| B | HOH515 |
| B | HOH565 |
| B | HOH619 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 405 |
| Chain | Residue |
| A | SER294 |
| A | SER356 |
| A | THR358 |
| A | NA408 |
| B | TYR298 |
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. YAmKANptpeILslLaglG |
| Chain | Residue | Details |
| A | TYR48-GLY66 |
| site_id | PS00879 |
| Number of Residues | 18 |
| Details | ODR_DC_2_2 Orn/DAP/Arg decarboxylases family 2 signature 2. AeemgmhLtDLDIGGGFP |
| Chain | Residue | Details |
| A | ALA204-PRO221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor; shared with dimeric partner","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
