3RW9
Crystal Structure of human Spermidine Synthase in Complex with decarboxylated S-adenosylhomocysteine
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 |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
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 |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE DSH A 303 |
Chain | Residue |
A | GLN49 |
A | VAL129 |
A | GLY154 |
A | ASP155 |
A | GLY156 |
A | ASP173 |
A | SER174 |
A | PRO180 |
A | ALA181 |
A | SER183 |
A | LEU184 |
A | GLN70 |
A | HOH436 |
A | GLN80 |
A | GLY101 |
A | GLY103 |
A | ASP104 |
A | CYS123 |
A | GLU124 |
A | ILE125 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE DSH B 303 |
Chain | Residue |
B | GLN49 |
B | GLN70 |
B | GLN80 |
B | GLY101 |
B | GLY103 |
B | ASP104 |
B | CYS123 |
B | GLU124 |
B | ILE125 |
B | VAL129 |
B | GLY154 |
B | ASP155 |
B | GLY156 |
B | ASP173 |
B | SER174 |
B | SER175 |
B | PRO180 |
B | ALA181 |
B | SER183 |
B | LEU184 |
B | HOH314 |
B | HOH396 |
Functional Information from PROSITE/UniProt
site_id | PS01330 |
Number of Residues | 14 |
Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLIIGGGdGgvLrE |
Chain | Residue | Details |
A | VAL97-GLU110 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP173 | |
B | ASP173 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | GLN49 | |
B | TYR79 | |
B | GLN80 | |
B | ASP104 | |
B | GLU124 | |
B | ASP155 | |
B | ASP173 | |
B | TYR241 | |
A | TYR79 | |
A | GLN80 | |
A | ASP104 | |
A | GLU124 | |
A | ASP155 | |
A | ASP173 | |
A | TYR241 | |
B | GLN49 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |