6O63
Crystal Structure of Arabidopsis thaliana Spermidine Synthase isoform 1 (AtSPDS1)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004766 | molecular_function | spermidine synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006595 | biological_process | polyamine metabolic process |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004766 | molecular_function | spermidine synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006595 | biological_process | polyamine metabolic process |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004766 | molecular_function | spermidine synthase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006595 | biological_process | polyamine metabolic process |
| C | 0008295 | biological_process | spermidine biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004766 | molecular_function | spermidine synthase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006595 | biological_process | polyamine metabolic process |
| D | 0008295 | biological_process | spermidine biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue PEG A 401 |
| Chain | Residue |
| A | VAL95 |
| A | HOH613 |
| A | GLN97 |
| A | TYR106 |
| A | ASP201 |
| A | SER202 |
| A | ASP204 |
| A | TYR270 |
| A | HOH535 |
| A | HOH555 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ARG101 |
| A | HOH571 |
| B | TRP239 |
| B | PHE324 |
| B | HOH573 |
| B | HOH623 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PEG B 401 |
| Chain | Residue |
| B | VAL95 |
| B | GLN97 |
| B | TYR106 |
| B | ASP201 |
| B | SER202 |
| B | ASP204 |
| B | TYR270 |
| B | HOH523 |
| B | HOH552 |
| B | HOH613 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | GLU151 |
| B | ILE152 |
| B | ASP182 |
| B | GLY183 |
| B | LEU212 |
| B | HOH531 |
| B | HOH592 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | ARG140 |
| B | HIS141 |
| B | ALA142 |
| B | SER143 |
| B | ILE296 |
| B | HOH585 |
| B | HOH600 |
| B | HOH610 |
| B | HOH626 |
| B | HOH654 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue PEG C 401 |
| Chain | Residue |
| C | GLN97 |
| C | TYR106 |
| C | ASP201 |
| C | SER202 |
| C | ASP204 |
| C | TYR270 |
| C | PRO271 |
| C | HOH533 |
| C | HOH570 |
| C | HOH587 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | PRO295 |
| C | ILE296 |
| C | ASP297 |
| C | TYR310 |
| C | ASN311 |
| C | ALA312 |
| C | GLU313 |
| C | HOH501 |
| C | HOH623 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue PEG D 401 |
| Chain | Residue |
| D | GLN97 |
| D | TYR106 |
| D | ASP201 |
| D | SER202 |
| D | ASP204 |
| D | TYR270 |
| D | HOH515 |
| D | HOH538 |
| D | HOH575 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| C | ARG101 |
| C | HOH614 |
| C | HOH652 |
| D | HOH542 |
| D | HOH640 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 403 |
| Chain | Residue |
| D | HIS141 |
| D | ALA142 |
| D | SER143 |
| D | HOH504 |
| D | HOH534 |
| D | HOH570 |
Functional Information from PROSITE/UniProt
| site_id | PS01330 |
| Number of Residues | 14 |
| Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLVIGGGdGgvLrE |
| Chain | Residue | Details |
| A | VAL124-GLU137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP201 | |
| B | ASP201 | |
| C | ASP201 | |
| D | ASP201 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| C | GLU151 | |
| C | ASP182 | |
| C | ASP201 | |
| C | TYR270 | |
| D | GLN76 | |
| D | TYR106 | |
| D | GLN107 | |
| D | ASP131 | |
| D | GLU151 | |
| D | ASP182 | |
| D | ASP201 | |
| D | TYR270 | |
| A | GLN76 | |
| A | TYR106 | |
| A | GLN107 | |
| A | ASP131 | |
| A | GLU151 | |
| A | ASP182 | |
| A | ASP201 | |
| A | TYR270 | |
| B | GLN76 | |
| B | TYR106 | |
| B | GLN107 | |
| B | ASP131 | |
| B | GLU151 | |
| B | ASP182 | |
| B | ASP201 | |
| B | TYR270 | |
| C | GLN76 | |
| C | TYR106 | |
| C | GLN107 | |
| C | ASP131 |
