Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004478 | molecular_function | methionine adenosyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0009087 | biological_process | methionine catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0048269 | cellular_component | methionine adenosyltransferase complex |
A | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA A 401 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 402 |
Chain | Residue |
A | GLU147 |
A | GLU216 |
A | LYS307 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE SAM A 501 |
Chain | Residue |
A | ASP116 |
A | ILE117 |
A | GLY133 |
A | ASP134 |
A | ASP179 |
A | LYS181 |
A | SER247 |
A | ARG249 |
A | PHE250 |
A | ASP258 |
A | LYS289 |
A | HOH644 |
A | HOH652 |
A | HOH687 |
A | HOH732 |
A | HOH753 |
A | HOH798 |
A | HIS29 |
A | PRO30 |
A | ALA55 |
A | GLU70 |
A | GLN113 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PG4 A 601 |
Chain | Residue |
A | GLN190 |
A | GLY193 |
A | ARG313 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 A 602 |
Chain | Residue |
A | GLU148 |
A | LYS159 |
A | TYR377 |
A | ARG382 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PG4 A 603 |
Chain | Residue |
A | THR146 |
A | GLU147 |
A | GLU211 |
A | ASP212 |
A | ILE213 |
A | LYS307 |
A | HOH738 |
Functional Information from PROSITE/UniProt
site_id | PS00376 |
Number of Residues | 11 |
Details | ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGlmfGY |
Chain | Residue | Details |
A | GLY131-TYR141 | |
site_id | PS00377 |
Number of Residues | 9 |
Details | ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD |
Chain | Residue | Details |
A | GLY278-ASP286 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU23 | |
Chain | Residue | Details |
A | HIS29 | |
A | ASP179 | |
A | SER247 | |
Chain | Residue | Details |
A | GLU57 | |
A | ASP258 | |
A | ALA281 | |
A | LYS285 | |
Chain | Residue | Details |
A | GLU70 | |
A | GLN113 | |
A | ARG264 | |
A | LYS289 | |
Chain | Residue | Details |
A | CYS120 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1fug |
Chain | Residue | Details |
A | ASP291 | |
A | LYS285 | |
A | LYS289 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fug |
Chain | Residue | Details |
A | ARG264 | |
A | LYS181 | |
A | LYS265 | |
A | HIS29 | |