6SW5
Crystal structure of the human S-adenosylmethionine synthetase 1 (ligand-free form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | L-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 | 0051259 | biological_process | protein complex oligomerization |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0009087 | biological_process | L-methionine catabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048269 | cellular_component | methionine adenosyltransferase complex |
| B | 0051259 | biological_process | protein complex oligomerization |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0009087 | biological_process | L-methionine catabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048269 | cellular_component | methionine adenosyltransferase complex |
| C | 0051259 | biological_process | protein complex oligomerization |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0009087 | biological_process | L-methionine catabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048269 | cellular_component | methionine adenosyltransferase complex |
| D | 0051259 | biological_process | protein complex oligomerization |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 401 |
| Chain | Residue |
| A | GLN317 |
| A | PHE333 |
| B | ARG313 |
| B | PEG1001 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | ALA276 |
| B | ALA276 |
| B | HIS277 |
| A | ILE267 |
| A | TYR271 |
| A | GLY273 |
| A | TRP274 |
| A | GLY275 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | MET138 |
| A | PHE139 |
| A | THR270 |
| A | HIS277 |
| A | GLY278 |
| A | PHE282 |
| A | HOH531 |
| A | HOH548 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLN187 |
| A | ARG199 |
| A | HOH556 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | GLU326 |
| A | HIS350 |
| A | PHE353 |
| A | LEU355 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ASP144 |
| A | THR146 |
| A | LYS307 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | GLY275 |
| A | ARG313 |
| A | HOH553 |
| B | PEG1001 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 1001 |
| Chain | Residue |
| A | LEU315 |
| A | TYR335 |
| A | PEG401 |
| A | EDO407 |
| B | GLY275 |
| B | TYR335 |
| B | HOH1147 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1002 |
| Chain | Residue |
| B | PHE139 |
| B | HIS277 |
| B | GLY278 |
| B | ALA295 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 1003 |
| Chain | Residue |
| B | THR146 |
| B | GLU148 |
| B | LYS159 |
| B | HOH1110 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | GLN36 |
| C | HIS89 |
| C | GLN372 |
| C | CYS376 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 402 |
| Chain | Residue |
| C | GLY275 |
| C | ARG313 |
| C | HOH532 |
| C | HOH557 |
| D | LEU315 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | GLU148 |
| C | PRO232 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| D | GLU326 |
| D | HIS350 |
| D | PHE353 |
| D | LEU355 |
| D | HOH515 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13444","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"23425511","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2OBV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






