3C6K
Crystal structure of human spermine synthase in complex with spermidine and 5-methylthioadenosine
Replaces: 2QFMFunctional 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 | 11 |
Details | BINDING SITE FOR RESIDUE SPD A 501 |
Chain | Residue |
A | ASP169 |
A | HOH537 |
A | HOH574 |
A | VAL170 |
A | ASN171 |
A | TYR179 |
A | ASP278 |
A | LEU279 |
A | TYR353 |
A | GLU355 |
A | TRP357 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SPD B 501 |
Chain | Residue |
B | ASP169 |
B | VAL170 |
B | ASN171 |
B | TYR179 |
B | ASP278 |
B | LEU279 |
B | TYR353 |
B | GLU355 |
B | TRP357 |
B | HOH522 |
B | HOH530 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SPD C 501 |
Chain | Residue |
C | ASP169 |
C | VAL170 |
C | ASN171 |
C | TYR179 |
C | ASP278 |
C | LEU279 |
C | TYR353 |
C | GLU355 |
C | TRP357 |
C | HOH752 |
C | HOH778 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SPD D 501 |
Chain | Residue |
D | ASP169 |
D | VAL170 |
D | ASN171 |
D | TYR179 |
D | ASP278 |
D | LEU279 |
D | TYR353 |
D | GLU355 |
D | TRP357 |
D | HOH687 |
D | HOH689 |
D | HOH692 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE MTA A 401 |
Chain | Residue |
A | GLN150 |
A | LEU164 |
A | LEU166 |
A | ASN171 |
A | GLY200 |
A | GLY202 |
A | ASP203 |
A | VAL221 |
A | GLU222 |
A | ILE223 |
A | ASP224 |
A | VAL227 |
A | ASP257 |
A | CYS258 |
A | ASP278 |
A | LEU279 |
A | THR280 |
A | ILE284 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE MTA B 401 |
Chain | Residue |
B | GLN150 |
B | LEU164 |
B | LEU166 |
B | GLY200 |
B | GLY201 |
B | GLY202 |
B | ASP203 |
B | VAL221 |
B | GLU222 |
B | ILE223 |
B | ASP224 |
B | VAL227 |
B | ASP257 |
B | CYS258 |
B | ASP278 |
B | LEU279 |
B | THR280 |
B | ILE284 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MTA C 401 |
Chain | Residue |
C | GLN150 |
C | LEU164 |
C | LEU166 |
C | GLY200 |
C | VAL221 |
C | GLU222 |
C | ILE223 |
C | ASP224 |
C | VAL227 |
C | ASP257 |
C | CYS258 |
C | ASP278 |
C | LEU279 |
C | THR280 |
C | ILE284 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MTA D 401 |
Chain | Residue |
D | ASN171 |
D | GLY200 |
D | GLY202 |
D | VAL221 |
D | GLU222 |
D | ILE223 |
D | VAL227 |
D | ASP257 |
D | CYS258 |
D | ASP278 |
D | LEU279 |
D | THR280 |
D | ILE284 |
D | GLN150 |
D | LEU164 |
D | LEU166 |
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 | VAL196-GLU209 |
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 | ASP278 | |
B | ASP278 | |
C | ASP278 | |
D | ASP278 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18367445 |
Chain | Residue | Details |
A | GLN150 | |
B | ASP203 | |
B | GLU222 | |
B | ASP257 | |
B | TYR353 | |
B | GLU355 | |
C | GLN150 | |
C | TYR179 | |
C | ASP203 | |
C | GLU222 | |
C | ASP257 | |
A | TYR179 | |
C | TYR353 | |
C | GLU355 | |
D | GLN150 | |
D | TYR179 | |
D | ASP203 | |
D | GLU222 | |
D | ASP257 | |
D | TYR353 | |
D | GLU355 | |
A | ASP203 | |
A | GLU222 | |
A | ASP257 | |
A | TYR353 | |
A | GLU355 | |
B | GLN150 | |
B | TYR179 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER59 | |
B | SER59 | |
C | SER59 | |
D | SER59 |