Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005730 | cellular_component | nucleolus |
| 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 | 0009505 | cellular_component | plant-type cell wall |
| A | 0009506 | cellular_component | plasmodesma |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005730 | cellular_component | nucleolus |
| 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 | 0009505 | cellular_component | plant-type cell wall |
| B | 0009506 | cellular_component | plasmodesma |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue PPK A 401 |
| Chain | Residue |
| A | HIS15 |
| A | HOH517 |
| A | HOH556 |
| A | HOH568 |
| A | HOH583 |
| A | HOH653 |
| A | HOH655 |
| A | HOH661 |
| B | ASP122 |
| B | GLY268 |
| B | ALA269 |
| A | ASP17 |
| B | LYS273 |
| B | ASP279 |
| B | HOH575 |
| B | HOH619 |
| A | LYS169 |
| A | ARG252 |
| A | LYS253 |
| A | MG402 |
| A | MG403 |
| A | K405 |
| A | SAM409 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP17 |
| A | LYS253 |
| A | PPK401 |
| A | HOH568 |
| A | HOH583 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | PPK401 |
| A | HOH655 |
| A | HOH661 |
| B | HOH575 |
| B | HOH619 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | HOH585 |
| A | HOH588 |
| B | PPK401 |
| B | HOH638 |
| B | HOH653 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue K A 405 |
| Chain | Residue |
| A | ASP246 |
| A | ALA247 |
| A | PPK401 |
| B | GLU43 |
| B | HOH631 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue MPO A 406 |
| Chain | Residue |
| A | ASP37 |
| A | LYS39 |
| A | HIS108 |
| A | PHE111 |
| A | THR112 |
| A | LYS113 |
| A | LYS355 |
| A | HOH522 |
| A | HOH526 |
| A | HOH723 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 407 |
| Chain | Residue |
| A | LYS338 |
| A | GLU339 |
| A | HOH508 |
| A | HOH542 |
| A | HOH561 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 408 |
| Chain | Residue |
| A | LYS91 |
| A | ASN180 |
| A | HOH552 |
| A | HOH776 |
| B | VAL94 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | binding site for residue SAM A 409 |
| Chain | Residue |
| A | HIS15 |
| A | PRO16 |
| A | ASP167 |
| A | LYS169 |
| A | SER235 |
| A | ARG237 |
| A | PHE238 |
| A | ASP246 |
| A | PPK401 |
| A | HOH556 |
| A | HOH615 |
| A | HOH673 |
| A | HOH679 |
| B | ALA41 |
| B | GLU56 |
| B | GLN99 |
| B | ASP102 |
| B | ILE103 |
| B | GLY121 |
| B | ASP122 |
| B | LYS277 |
| B | ILE310 |
| B | HOH629 |
| B | HOH781 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 410 |
| site_id | AD2 |
| Number of Residues | 23 |
| Details | binding site for residue PPK B 401 |
| Chain | Residue |
| B | ARG252 |
| B | LYS253 |
| B | MG404 |
| B | K406 |
| B | SAM409 |
| B | HOH542 |
| B | HOH546 |
| B | HOH565 |
| B | HOH586 |
| B | HOH624 |
| B | HOH638 |
| B | HOH653 |
| A | ASP122 |
| A | GLY268 |
| A | ALA269 |
| A | LYS273 |
| A | ASP279 |
| A | MG404 |
| A | HOH585 |
| A | HOH588 |
| B | HIS15 |
| B | ASP17 |
| B | LYS169 |
| site_id | AD3 |
| Number of Residues | 8 |
| Details | binding site for residue PDO B 402 |
| Chain | Residue |
| B | LYS211 |
| B | GLU221 |
| B | LEU224 |
| B | HOH506 |
| B | HOH539 |
| B | HOH618 |
| B | HOH762 |
| B | HOH888 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue PGR B 403 |
| Chain | Residue |
| B | THR146 |
| B | ALA150 |
| B | TYR368 |
| B | ARG373 |
| B | HOH505 |
| B | HOH885 |
| B | HOH991 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | ASP17 |
| B | LYS253 |
| B | PPK401 |
| B | HOH565 |
| B | HOH586 |
| site_id | AD6 |
| Number of Residues | 13 |
| Details | binding site for residue PE8 B 405 |
| Chain | Residue |
| A | GLY261 |
| A | ASP321 |
| A | HOH848 |
| B | PHE4 |
| B | ASN178 |
| B | GLY261 |
| B | TRP262 |
| B | HOH774 |
| B | HOH798 |
| B | HOH820 |
| B | HOH850 |
| B | HOH871 |
| B | HOH959 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue K B 406 |
| Chain | Residue |
| A | GLU43 |
| A | HOH616 |
| B | ASP246 |
| B | ALA247 |
| B | PPK401 |
| B | HOH586 |
| site_id | AD8 |
| Number of Residues | 11 |
| Details | binding site for residue MPO B 407 |
| Chain | Residue |
| B | ASP37 |
| B | LYS39 |
| B | HIS108 |
| B | PHE111 |
| B | THR112 |
| B | LYS113 |
| B | ARG114 |
| B | LYS355 |
| B | HOH657 |
| B | HOH660 |
| B | HOH712 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue PGE B 408 |
| Chain | Residue |
| B | ARG162 |
| B | HOH501 |
| B | HOH879 |
| site_id | AE1 |
| Number of Residues | 23 |
| Details | binding site for residue SAM B 409 |
| Chain | Residue |
| A | ALA41 |
| A | GLU56 |
| A | GLN99 |
| A | ASP102 |
| A | ILE103 |
| A | ASP122 |
| A | LYS277 |
| A | ILE310 |
| A | HOH590 |
| A | HOH782 |
| B | HIS15 |
| B | PRO16 |
| B | ASP167 |
| B | LYS169 |
| B | SER235 |
| B | ARG237 |
| B | PHE238 |
| B | ASP246 |
| B | PPK401 |
| B | HOH542 |
| B | HOH630 |
| B | HOH674 |
| B | HOH727 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 410 |
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 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU9 | |
| B | GLU9 | |
| Chain | Residue | Details |
| A | HIS15 | |
| A | ASP167 | |
| A | SER235 | |
| B | HIS15 | |
| B | ASP167 | |
| B | SER235 | |
| Chain | Residue | Details |
| A | GLU43 | |
| A | ASP246 | |
| A | ALA269 | |
| A | LYS273 | |
| B | GLU43 | |
| B | ASP246 | |
| B | ALA269 | |
| B | LYS273 | |
| Chain | Residue | Details |
| A | GLU56 | |
| A | GLN99 | |
| A | ARG252 | |
| A | LYS277 | |
| B | GLU56 | |
| B | GLN99 | |
| B | ARG252 | |
| B | LYS277 | |
