6SW5
Crystal structure of the human S-adenosylmethionine synthetase 1 (ligand-free form)
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 |
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 | 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 | 0051289 | biological_process | protein homotetramerization |
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 | 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 | 0051289 | biological_process | protein homotetramerization |
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 | 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 | 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: BINDING => ECO:0000250|UniProtKB:P13444 |
Chain | Residue | Details |
A | GLU23 | |
B | GLU23 | |
C | GLU23 | |
D | GLU23 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: in other chain => ECO:0000305|PubMed:23425511, ECO:0007744|PDB:2OBV |
Chain | Residue | Details |
A | HIS29 | |
D | HIS29 | |
D | ASP179 | |
D | SER247 | |
A | ASP179 | |
A | SER247 | |
B | HIS29 | |
B | ASP179 | |
B | SER247 | |
C | HIS29 | |
C | ASP179 | |
C | SER247 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | GLU57 | |
C | ASP258 | |
C | ALA281 | |
C | LYS285 | |
D | GLU57 | |
D | ASP258 | |
D | ALA281 | |
D | LYS285 | |
A | ASP258 | |
A | ALA281 | |
A | LYS285 | |
B | GLU57 | |
B | ASP258 | |
B | ALA281 | |
B | LYS285 | |
C | GLU57 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: in other chain => ECO:0000250|UniProtKB:P0A817 |
Chain | Residue | Details |
A | GLU70 | |
C | GLN113 | |
C | ARG264 | |
C | LYS289 | |
D | GLU70 | |
D | GLN113 | |
D | ARG264 | |
D | LYS289 | |
A | GLN113 | |
A | ARG264 | |
A | LYS289 | |
B | GLU70 | |
B | GLN113 | |
B | ARG264 | |
B | LYS289 | |
C | GLU70 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P13444 |
Chain | Residue | Details |
A | CYS120 | |
B | CYS120 | |
C | CYS120 | |
D | CYS120 |