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 | 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 | 0008295 | biological_process | spermidine biosynthetic process |
B | 0008923 | molecular_function | lysine decarboxylase activity |
B | 0009446 | biological_process | putrescine biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0033387 | biological_process | putrescine biosynthetic process from 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 | ACT_SITE: Proton donor; shared with dimeric partner => ECO:0000250 |
Chain | Residue | Details |
A | CYS323 | |
B | CYS323 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS51 | |
B | LYS51 |