Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP279 |
| A | HOH512 |
| A | HOH567 |
| A | HOH570 |
| A | HOH579 |
| A | HOH841 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | HOH902 |
| A | HOH914 |
| A | HOH980 |
| A | HOH525 |
| A | HOH557 |
| A | HOH566 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ARG70 |
| A | VAL92 |
| A | LYS331 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLY121 |
| A | ASP122 |
| A | THR276 |
| A | LYS277 |
| A | VAL278 |
| A | HOH501 |
| A | HOH507 |
| A | HOH508 |
| A | HOH799 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASP279 |
| B | HOH539 |
| B | HOH547 |
| B | HOH610 |
| B | HOH640 |
| B | HOH841 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | HOH563 |
| B | HOH883 |
| B | HOH915 |
| B | HOH971 |
| B | HOH974 |
| B | HOH977 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 403 |
Functional Information from PROSITE/UniProt
| site_id | PS00376 |
| Number of Residues | 11 |
| Details | ADOMET_SYNTHASE_1 S-adenosylmethionine synthase signature 1. GAGDQGhmfGY |
| Chain | Residue | Details |
| A | GLY119-TYR129 | |
| site_id | PS00377 |
| Number of Residues | 9 |
| Details | ADOMET_SYNTHASE_2 S-adenosylmethionine synthase signature 2. GGGAFSgKD |
| Chain | Residue | Details |
| A | GLY266-ASP274 | |
