1RG9
S-Adenosylmethionine synthetase complexed with SAM and PPNP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| 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 | 0030955 | molecular_function | potassium ion binding |
| A | 0033353 | biological_process | S-adenosylmethionine cycle |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| 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 | 0030955 | molecular_function | potassium ion binding |
| B | 0033353 | biological_process | S-adenosylmethionine cycle |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0033353 | biological_process | S-adenosylmethionine cycle |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0033353 | biological_process | S-adenosylmethionine cycle |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K A 386 |
| Chain | Residue |
| A | ASP238 |
| A | CYS239 |
| A | PPK384 |
| B | GLU42 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 387 |
| Chain | Residue |
| A | GLU8 |
| A | LYS165 |
| A | PPK384 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 388 |
| Chain | Residue |
| A | ASP16 |
| A | PPK384 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K B 486 |
| Chain | Residue |
| A | GLU42 |
| B | ASP238 |
| B | CYS239 |
| B | PPK484 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 487 |
| Chain | Residue |
| B | GLU8 |
| B | LYS165 |
| B | PPK484 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 488 |
| Chain | Residue |
| B | ASP16 |
| B | PPK484 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 586 |
| Chain | Residue |
| C | ASP238 |
| C | CYS239 |
| C | PPK584 |
| D | GLU42 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 587 |
| Chain | Residue |
| C | LYS165 |
| C | PPK584 |
| D | ASP118 |
| D | ASP271 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 588 |
| Chain | Residue |
| C | ASP16 |
| C | PPK584 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 686 |
| Chain | Residue |
| C | GLU42 |
| D | ASP238 |
| D | CYS239 |
| D | PPK684 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 687 |
| Chain | Residue |
| C | ASP271 |
| D | LYS165 |
| D | PPK684 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 688 |
| Chain | Residue |
| D | ASP16 |
| D | PPK684 |
| site_id | BC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAM A 385 |
| Chain | Residue |
| A | HIS14 |
| A | PRO15 |
| A | ASP163 |
| A | LYS165 |
| A | SER186 |
| A | ARG229 |
| A | PHE230 |
| A | ASP238 |
| A | PPK384 |
| A | HOH389 |
| A | HOH390 |
| A | HOH391 |
| A | HOH392 |
| B | ALA40 |
| B | GLU55 |
| B | GLN98 |
| B | ASP101 |
| B | ILE102 |
| B | GLY117 |
| B | ASP118 |
| B | LYS269 |
| B | ILE302 |
| site_id | BC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE SAM B 485 |
| Chain | Residue |
| A | ALA40 |
| A | GLU55 |
| A | GLN98 |
| A | ASP101 |
| A | ILE102 |
| A | GLY117 |
| A | ASP118 |
| A | LYS269 |
| A | ILE302 |
| A | HOH393 |
| B | HIS14 |
| B | PRO15 |
| B | ASP163 |
| B | LYS165 |
| B | SER186 |
| B | THR227 |
| B | ARG229 |
| B | PHE230 |
| B | ASP238 |
| B | PPK484 |
| B | HOH500 |
| site_id | BC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAM C 585 |
| Chain | Residue |
| D | ASP118 |
| D | LYS269 |
| D | ILE302 |
| C | HIS14 |
| C | PRO15 |
| C | ASP163 |
| C | LYS165 |
| C | THR227 |
| C | ARG229 |
| C | PHE230 |
| C | ASP238 |
| C | PPK584 |
| C | HOH700 |
| C | HOH702 |
| C | HOH711 |
| C | HOH716 |
| D | ALA40 |
| D | GLU55 |
| D | GLN98 |
| D | ASP101 |
| D | ILE102 |
| D | GLY117 |
| site_id | BC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SAM C 685 |
| Chain | Residue |
| C | ALA40 |
| C | GLU55 |
| C | GLN98 |
| C | ASP101 |
| C | ILE102 |
| C | GLY117 |
| C | ASP118 |
| C | LYS269 |
| C | ILE302 |
| C | HOH900 |
| C | HOH902 |
| D | HIS14 |
| D | ASP163 |
| D | LYS165 |
| D | THR227 |
| D | ARG229 |
| D | PHE230 |
| D | ASP238 |
| D | PPK684 |
| D | HOH916 |
| site_id | BC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PPK A 384 |
| Chain | Residue |
| A | HIS14 |
| A | ASP16 |
| A | LYS165 |
| A | ASP238 |
| A | ARG244 |
| A | LYS245 |
| A | SAM385 |
| A | K386 |
| A | MG387 |
| A | MG388 |
| B | ASP118 |
| B | GLY259 |
| B | GLY260 |
| B | ALA261 |
| B | LYS265 |
| B | ASP271 |
| site_id | BC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PPK B 484 |
| Chain | Residue |
| A | ASP118 |
| A | GLY259 |
| A | GLY260 |
| A | ALA261 |
| A | LYS265 |
| A | ASP271 |
| B | HIS14 |
| B | ASP16 |
| B | LYS165 |
| B | ASP238 |
| B | ARG244 |
| B | LYS245 |
| B | SAM485 |
| B | K486 |
| B | MG487 |
| B | MG488 |
| site_id | CC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PPK C 584 |
| Chain | Residue |
| C | HIS14 |
| C | ASP16 |
| C | LYS165 |
| C | ASP238 |
| C | ARG244 |
| C | LYS245 |
| C | SAM585 |
| C | K586 |
| C | MG588 |
| D | ASP118 |
| D | GLY259 |
| D | GLY260 |
| D | ALA261 |
| D | LYS265 |
| D | ASP271 |
| D | MG587 |
| site_id | CC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PPK D 684 |
| Chain | Residue |
| C | ASP118 |
| C | GLY259 |
| C | GLY260 |
| C | ALA261 |
| C | LYS265 |
| C | ASP271 |
| C | SAM685 |
| C | MG687 |
| D | HIS14 |
| D | ASP16 |
| D | LYS165 |
| D | ARG244 |
| D | LYS245 |
| D | K686 |
| D | MG688 |
| D | HOH930 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9 |
| Chain | Residue | Details |
| A | PRO15 | |
| B | SER99 | |
| B | ALA164 | |
| B | PHE230 | |
| B | LYS245 | |
| B | VAL270 | |
| C | PRO15 | |
| C | ILE56 | |
| C | SER99 | |
| C | ALA164 | |
| C | PHE230 | |
| A | ILE56 | |
| C | LYS245 | |
| C | VAL270 | |
| D | PRO15 | |
| D | ILE56 | |
| D | SER99 | |
| D | ALA164 | |
| D | PHE230 | |
| D | LYS245 | |
| D | VAL270 | |
| A | SER99 | |
| A | ALA164 | |
| A | PHE230 | |
| A | LYS245 | |
| A | VAL270 | |
| B | PRO15 | |
| B | ILE56 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9 |
| Chain | Residue | Details |
| A | LYS17 | |
| D | LYS17 | |
| D | PHE262 | |
| D | ASP266 | |
| A | PHE262 | |
| A | ASP266 | |
| B | LYS17 | |
| B | PHE262 | |
| B | ASP266 | |
| C | LYS17 | |
| C | PHE262 | |
| C | ASP266 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0000305|PubMed:7629147, ECO:0007744|PDB:1MXC, ECO:0007744|PDB:1P7L, ECO:0007744|PDB:1RG9 |
| Chain | Residue | Details |
| A | THR43 | |
| B | THR43 | |
| C | THR43 | |
| D | THR43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00086, ECO:0000269|PubMed:14967023, ECO:0007744|PDB:1P7L |
| Chain | Residue | Details |
| A | CYS239 | |
| B | CYS239 | |
| C | CYS239 | |
| D | CYS239 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | HIS3 | |
| B | HIS3 | |
| C | HIS3 | |
| D | HIS3 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | LYS245 | |
| A | HIS14 | |
| A | LYS165 | |
| A | ARG244 | |
| B | LYS269 | |
| B | LYS265 | |
| B | ASP271 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | LYS269 | |
| A | LYS265 | |
| A | ASP271 | |
| B | LYS245 | |
| B | HIS14 | |
| B | LYS165 | |
| B | ARG244 |
| site_id | CSA3 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| C | LYS245 | |
| C | HIS14 | |
| C | LYS165 | |
| C | ARG244 | |
| D | LYS269 | |
| D | LYS265 | |
| D | ASP271 |
| site_id | CSA4 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| C | LYS269 | |
| C | LYS265 | |
| C | ASP271 | |
| D | LYS245 | |
| D | HIS14 | |
| D | LYS165 | |
| D | ARG244 |
