3IML
Crystal Structure Of S-Adenosylmethionine Synthetase From Burkholderia Pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086 |
| Chain | Residue | Details |
| A | HIS16 | |
| B | GLN100 | |
| B | ASP167 | |
| B | ARG233 | |
| B | ARG248 | |
| B | LYS273 | |
| C | HIS16 | |
| C | GLU57 | |
| C | GLN100 | |
| C | ASP167 | |
| C | ARG233 | |
| A | GLU57 | |
| C | ARG248 | |
| C | LYS273 | |
| D | HIS16 | |
| D | GLU57 | |
| D | GLN100 | |
| D | ASP167 | |
| D | ARG233 | |
| D | ARG248 | |
| D | LYS273 | |
| A | GLN100 | |
| A | ASP167 | |
| A | ARG233 | |
| A | ARG248 | |
| A | LYS273 | |
| B | HIS16 | |
| B | GLU57 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086 |
| Chain | Residue | Details |
| A | ASP18 | |
| B | LYS269 | |
| C | ASP18 | |
| C | GLU44 | |
| C | ASP242 | |
| C | ALA265 | |
| C | LYS269 | |
| D | ASP18 | |
| D | GLU44 | |
| D | ASP242 | |
| D | ALA265 | |
| A | GLU44 | |
| D | LYS269 | |
| A | ASP242 | |
| A | ALA265 | |
| A | LYS269 | |
| B | ASP18 | |
| B | GLU44 | |
| B | ASP242 | |
| B | ALA265 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | LYS273 | |
| A | LYS269 | |
| A | ASP275 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| B | LYS273 | |
| B | LYS269 | |
| B | ASP275 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| C | LYS273 | |
| C | LYS269 | |
| C | ASP275 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| D | LYS273 | |
| D | LYS269 | |
| D | ASP275 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | ARG248 | |
| A | LYS249 | |
| A | LYS169 | |
| A | HIS16 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| B | ARG248 | |
| B | LYS249 | |
| B | LYS169 | |
| B | HIS16 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| C | ARG248 | |
| C | LYS249 | |
| C | LYS169 | |
| C | HIS16 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| D | ARG248 | |
| D | LYS249 | |
| D | LYS169 | |
| D | HIS16 |
