1JL0
Structure of a Human S-Adenosylmethionine Decarboxylase Self-processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing as Revealed by the H243A Mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004014 | molecular_function | adenosylmethionine decarboxylase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0006595 | biological_process | polyamine metabolic process |
A | 0006597 | biological_process | spermine biosynthetic process |
A | 0008295 | biological_process | spermidine biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019810 | molecular_function | putrescine binding |
A | 0042802 | molecular_function | identical protein binding |
B | 0004014 | molecular_function | adenosylmethionine decarboxylase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0006595 | biological_process | polyamine metabolic process |
B | 0006597 | biological_process | spermine biosynthetic process |
B | 0008295 | biological_process | spermidine biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019810 | molecular_function | putrescine binding |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PUT A 401 |
Chain | Residue |
A | LEU13 |
A | HOH3394 |
A | GLU15 |
A | PHE111 |
A | ASP174 |
A | THR176 |
A | PHE285 |
A | TYR318 |
A | HOH3001 |
A | HOH3018 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRS A 402 |
Chain | Residue |
A | HIS5 |
A | PHE7 |
A | CYS226 |
A | PRO246 |
A | GLU247 |
A | HOH3075 |
A | HOH3220 |
A | HOH3361 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PUT B 401 |
Chain | Residue |
B | LEU13 |
B | GLU15 |
B | PHE111 |
B | ASP174 |
B | THR176 |
B | TYR318 |
B | HOH503 |
B | HOH504 |
B | HOH514 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRS B 402 |
Chain | Residue |
B | HIS5 |
B | CYS226 |
B | PRO246 |
B | GLU247 |
B | HOH587 |
B | HOH733 |
Functional Information from PROSITE/UniProt
site_id | PS01336 |
Number of Residues | 11 |
Details | ADOMETDC S-adenosylmethionine decarboxylase signature. AYVLSESSMFV |
Chain | Residue | Details |
A | ALA62-VAL72 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:1917972 |
Chain | Residue | Details |
A | GLU8 | |
A | GLU11 | |
B | GLU8 | |
B | GLU11 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:11583147 |
Chain | Residue | Details |
A | SER68 | |
B | SER68 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor; for catalytic activity => ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:11583147 |
Chain | Residue | Details |
A | CYS82 | |
B | CYS82 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor; for processing activity => ECO:0000269|PubMed:11583147 |
Chain | Residue | Details |
A | SER229 | |
A | ALA243 | |
B | SER229 | |
B | ALA243 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11583147 |
Chain | Residue | Details |
A | PHE7 | |
A | GLU67 | |
A | PHE223 | |
A | GLU247 | |
B | PHE7 | |
B | GLU67 | |
B | PHE223 | |
B | GLU247 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Cleavage (non-hydrolytic); by autolysis => ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270 |
Chain | Residue | Details |
A | GLU67 | |
B | GLU67 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Pyruvic acid (Ser); by autocatalysis => ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270 |
Chain | Residue | Details |
A | SER68 | |
B | SER68 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER298 | |
B | SER298 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1jen |
Chain | Residue | Details |
A | ALA243 | |
A | SER229 | |
A | CYS82 | |
B | GLU11 | |
B | GLU67 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1jen |
Chain | Residue | Details |
A | GLU11 | |
A | GLU67 | |
B | SER229 | |
B | ALA243 | |
B | CYS82 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 575 |
Chain | Residue | Details |
A | GLU67 | |
A | SER68 | covalently attached, electron shuttle |
A | CYS82 | proton shuttle (general acid/base) |
A | SER229 | |
A | ALA243 |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 575 |
Chain | Residue | Details |
B | GLU67 | |
B | SER68 | covalently attached, electron shuttle |
B | CYS82 | proton shuttle (general acid/base) |
B | SER229 | |
B | ALA243 |