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 |
A | GLN76 | |
B | TYR106 | |
B | GLN107 | |
B | ASP131 | |
B | GLU151 | |
B | ASP182 | |
B | ASP201 | |
B | TYR270 | |
C | GLN76 | |
C | TYR106 | |
C | GLN107 | |
A | TYR106 | |
C | ASP131 | |
C | GLU151 | |
C | ASP182 | |
C | ASP201 | |
C | TYR270 | |
D | GLN76 | |
D | TYR106 | |
D | GLN107 | |
D | ASP131 | |
D | GLU151 | |
A | GLN107 | |
D | ASP182 | |
D | ASP201 | |
D | TYR270 | |
A | ASP131 | |
A | GLU151 | |
A | ASP182 | |
A | ASP201 | |
A | TYR270 | |
B | GLN76 |