3C6M
Crystal structure of human spermine synthase in complex with spermine and 5-methylthioadenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006555 | biological_process | methionine metabolic process |
| A | 0006595 | biological_process | polyamine metabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0006597 | biological_process | spermine biosynthetic process |
| A | 0008215 | biological_process | spermine metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016768 | molecular_function | spermine synthase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006555 | biological_process | methionine metabolic process |
| B | 0006595 | biological_process | polyamine metabolic process |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0006597 | biological_process | spermine biosynthetic process |
| B | 0008215 | biological_process | spermine metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016768 | molecular_function | spermine synthase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| C | 0005829 | cellular_component | cytosol |
| C | 0006555 | biological_process | methionine metabolic process |
| C | 0006595 | biological_process | polyamine metabolic process |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0006597 | biological_process | spermine biosynthetic process |
| C | 0008215 | biological_process | spermine metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016768 | molecular_function | spermine synthase activity |
| C | 0070062 | cellular_component | extracellular exosome |
| D | 0005829 | cellular_component | cytosol |
| D | 0006555 | biological_process | methionine metabolic process |
| D | 0006595 | biological_process | polyamine metabolic process |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0006597 | biological_process | spermine biosynthetic process |
| D | 0008215 | biological_process | spermine metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016768 | molecular_function | spermine synthase activity |
| D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SPM A 501 |
| Chain | Residue |
| A | TRP124 |
| A | LEU277 |
| A | TYR351 |
| A | GLU353 |
| A | TRP355 |
| A | HOH571 |
| A | HOH576 |
| A | PRO125 |
| A | TYR134 |
| A | ASP167 |
| A | VAL168 |
| A | ASN169 |
| A | TYR177 |
| A | ASP201 |
| A | ASP276 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SPM B 501 |
| Chain | Residue |
| B | ASP167 |
| B | VAL168 |
| B | ASN169 |
| B | TYR177 |
| B | ASP201 |
| B | ASP276 |
| B | LEU277 |
| B | GLN315 |
| B | TYR351 |
| B | GLU353 |
| B | TRP355 |
| B | MTA401 |
| B | HOH524 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SPM C 501 |
| Chain | Residue |
| C | ASP167 |
| C | VAL168 |
| C | ASN169 |
| C | TYR177 |
| C | ASP201 |
| C | ASP276 |
| C | LEU277 |
| C | GLN315 |
| C | TYR351 |
| C | GLU353 |
| C | TRP355 |
| C | MTA401 |
| C | HOH527 |
| C | HOH536 |
| C | HOH563 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SPM D 501 |
| Chain | Residue |
| D | TRP124 |
| D | THR126 |
| D | TYR134 |
| D | ASP167 |
| D | VAL168 |
| D | ASN169 |
| D | TYR177 |
| D | ASP201 |
| D | ASP276 |
| D | GLN315 |
| D | TYR351 |
| D | GLU353 |
| D | TRP355 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTA A 401 |
| Chain | Residue |
| A | GLN148 |
| A | LEU162 |
| A | LEU164 |
| A | ASN169 |
| A | GLY198 |
| A | GLY199 |
| A | GLY200 |
| A | ASP201 |
| A | VAL219 |
| A | GLU220 |
| A | ILE221 |
| A | ASP222 |
| A | VAL225 |
| A | ASP255 |
| A | CYS256 |
| A | ASP276 |
| A | LEU277 |
| A | THR278 |
| A | ILE282 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTA B 401 |
| Chain | Residue |
| B | GLN148 |
| B | LEU162 |
| B | LEU164 |
| B | ASN169 |
| B | GLY198 |
| B | GLY199 |
| B | ASP201 |
| B | VAL219 |
| B | GLU220 |
| B | ILE221 |
| B | ASP222 |
| B | VAL225 |
| B | ASP255 |
| B | CYS256 |
| B | ASP276 |
| B | LEU277 |
| B | THR278 |
| B | ILE282 |
| B | SPM501 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTA C 401 |
| Chain | Residue |
| C | GLY199 |
| C | GLY200 |
| C | ASP201 |
| C | VAL219 |
| C | GLU220 |
| C | ILE221 |
| C | VAL225 |
| C | ASP255 |
| C | CYS256 |
| C | ASP276 |
| C | LEU277 |
| C | THR278 |
| C | ILE282 |
| C | SPM501 |
| C | GLN148 |
| C | LEU162 |
| C | LEU164 |
| C | ASN169 |
| C | GLY198 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE MTA D 401 |
| Chain | Residue |
| D | GLN148 |
| D | LEU164 |
| D | ASN169 |
| D | GLY198 |
| D | GLY199 |
| D | GLY200 |
| D | ASP201 |
| D | VAL219 |
| D | GLU220 |
| D | ILE221 |
| D | VAL225 |
| D | ASP255 |
| D | CYS256 |
| D | ASP276 |
| D | LEU277 |
| D | THR278 |
| D | ILE282 |
Functional Information from PROSITE/UniProt
| site_id | PS01330 |
| Number of Residues | 14 |
| Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLILGGGdGgiLcE |
| Chain | Residue | Details |
| A | VAL194-GLU207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00354, ECO:0000269|PubMed:18367445 |
| Chain | Residue | Details |
| A | ASP276 | |
| B | ASP276 | |
| C | ASP276 | |
| D | ASP276 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18367445 |
| Chain | Residue | Details |
| A | GLN148 | |
| B | ASP201 | |
| B | GLU220 | |
| B | ASP255 | |
| B | TYR351 | |
| B | GLU353 | |
| C | GLN148 | |
| C | TYR177 | |
| C | ASP201 | |
| C | GLU220 | |
| C | ASP255 | |
| A | TYR177 | |
| C | TYR351 | |
| C | GLU353 | |
| D | GLN148 | |
| D | TYR177 | |
| D | ASP201 | |
| D | GLU220 | |
| D | ASP255 | |
| D | TYR351 | |
| D | GLU353 | |
| A | ASP201 | |
| A | GLU220 | |
| A | ASP255 | |
| A | TYR351 | |
| A | GLU353 | |
| B | GLN148 | |
| B | TYR177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER57 | |
| B | SER57 | |
| C | SER57 | |
| D | SER57 |
