1O93
Methionine Adenosyltransferase complexed with ATP and a L-methionine analogue
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 | 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 | 0016363 | cellular_component | nuclear matrix |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043531 | molecular_function | ADP binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048269 | cellular_component | methionine adenosyltransferase complex |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0065003 | biological_process | protein-containing complex assembly |
| 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 | 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 | 0016363 | cellular_component | nuclear matrix |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043531 | molecular_function | ADP binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048269 | cellular_component | methionine adenosyltransferase complex |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0065003 | biological_process | protein-containing complex assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A1400 |
| Chain | Residue |
| A | LYS182 |
| A | VAL205 |
| A | SER207 |
| A | MG1401 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A1401 |
| Chain | Residue |
| A | SER248 |
| A | PO41400 |
| B | ASP135 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A1402 |
| Chain | Residue |
| B | ATP1397 |
| A | LYS182 |
| A | LIS1398 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A1403 |
| Chain | Residue |
| A | GLU24 |
| A | LYS266 |
| A | HOH2001 |
| B | ATP1397 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A1404 |
| Chain | Residue |
| A | GLY264 |
| A | ILE267 |
| B | ARG265 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B1399 |
| Chain | Residue |
| A | ARG265 |
| A | LYS266 |
| A | HOH2003 |
| B | GLY280 |
| B | ALA282 |
| B | LYS286 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE K B1405 |
| Chain | Residue |
| B | SER284 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LIS A1398 |
| Chain | Residue |
| A | ARG250 |
| A | PHE251 |
| A | MG1402 |
| B | ATP1397 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ATP B1397 |
| Chain | Residue |
| A | HIS30 |
| A | PRO31 |
| A | ASP180 |
| A | LYS182 |
| A | GLY258 |
| A | ASP259 |
| A | LYS266 |
| A | LIS1398 |
| A | MG1402 |
| A | MG1403 |
| B | ALA56 |
| B | GLU71 |
| B | LYS290 |
| B | HOH2013 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O93","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P0A817","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"10873471","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1QM4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12888348","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1O92","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O9T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | LYS266 | |
| A | HIS30 | |
| A | LYS182 | |
| A | ARG265 | |
| B | LYS286 | |
| B | ASP292 | |
| B | LYS290 |
| site_id | CSA2 |
| Number of Residues | 7 |
| Details | Annotated By Reference To The Literature 1fug |
| Chain | Residue | Details |
| A | LYS286 | |
| A | ASP292 | |
| A | LYS290 | |
| B | LYS266 | |
| B | HIS30 | |
| B | LYS182 | |
| B | ARG265 |






