Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 404 |
| Chain | Residue |
| A | ASP259 |
| A | HOH447 |
| A | HOH448 |
| A | HOH482 |
| A | HOH506 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 405 |
| Chain | Residue |
| A | HOH454 |
| A | HOH455 |
| A | HOH478 |
| A | ASP394 |
| A | ASP397 |
| A | ASP398 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 406 |
| Chain | Residue |
| A | HIS158 |
| A | ARG162 |
| A | GLY382 |
| A | ARG383 |
| A | THR384 |
| A | ASP385 |
| A | HOH464 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 407 |
| Chain | Residue |
| A | ARG41 |
| A | ALA43 |
| A | GLU58 |
| A | VAL59 |
| A | THR60 |
| A | LYS290 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| B | ASP259 |
| B | HOH442 |
| B | HOH466 |
| B | HOH490 |
| B | HOH545 |
| B | HOH604 |
| B | HOH611 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 405 |
| Chain | Residue |
| B | HIS158 |
| B | ARG162 |
| B | GLY382 |
| B | ARG383 |
| B | THR384 |
| B | ASP385 |
| B | HOH535 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 406 |
| Chain | Residue |
| A | ARG363 |
| A | ASP364 |
| B | ASP364 |
| B | ASP394 |
| B | LYS395 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 407 |
| Chain | Residue |
| A | ASP364 |
| A | ASP394 |
| A | LYS395 |
| B | ARG363 |
| B | ASP364 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 408 |
| Chain | Residue |
| B | ARG41 |
| B | VAL42 |
| B | ALA43 |
| B | GLU58 |
| B | VAL59 |
| B | THR60 |
| B | LYS290 |
| B | HOH485 |
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 | GLY279-ASP287 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00086","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00086","evidenceCode":"ECO:0000255"}]} |
