6RKA
Inter-dimeric interface controls function and stability of S-methionine adenosyltransferase from U. urealiticum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue ATP A 401 |
| Chain | Residue |
| A | HIS16 |
| A | ARG237 |
| A | LYS238 |
| B | ASP113 |
| B | GLY252 |
| B | GLY253 |
| B | ALA254 |
| B | LYS258 |
| B | ASP264 |
| A | PRO17 |
| A | ASP18 |
| A | ASP158 |
| A | LYS160 |
| A | SER180 |
| A | SER220 |
| A | ARG222 |
| A | ASP231 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue SAM B 401 |
| Chain | Residue |
| A | ALA42 |
| A | GLU57 |
| A | GLN93 |
| A | ILE97 |
| A | GLY112 |
| A | ASP113 |
| A | LYS262 |
| A | ILE295 |
| B | HIS16 |
| B | PRO17 |
| B | ASP158 |
| B | LYS160 |
| B | SER220 |
| B | ARG222 |
| B | PHE223 |
| B | GLY230 |
| B | ASP231 |
| B | ATP402 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue ATP B 402 |
| Chain | Residue |
| A | ASP96 |
| A | ILE97 |
| A | ASP113 |
| A | ALA254 |
| A | LYS258 |
| A | ASP264 |
| A | ILE295 |
| B | HIS16 |
| B | PRO17 |
| B | ASP18 |
| B | ASP158 |
| B | LYS160 |
| B | SER220 |
| B | ARG222 |
| B | PHE223 |
| B | ASP231 |
| B | ARG237 |
| B | LYS238 |
| B | SAM401 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 401 |
| Chain | Residue |
| C | HIS16 |
| C | ASP18 |
| C | LYS160 |
| C | LYS238 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue SAM D 401 |
| Chain | Residue |
| C | ALA42 |
| C | GLU57 |
| C | GLN93 |
| C | ASP96 |
| C | ILE97 |
| C | ASP113 |
| C | LYS262 |
| C | ILE295 |
| D | HIS16 |
| D | PRO17 |
| D | ASP158 |
| D | LYS160 |
| D | SER220 |
| D | ARG222 |
| D | PHE223 |
| D | ILE225 |
| D | ASP231 |
| D | PO4402 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 D 402 |
| Chain | Residue |
| C | ASP113 |
| D | HIS16 |
| D | ASP18 |
| D | LYS160 |
| D | LYS238 |
| D | SAM401 |
Functional Information from PROSITE/UniProt
