6S81
Crystal structure of methionine adenosyltransferase from Pyrococcus furiosus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004478 | molecular_function | methionine adenosyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004478 | molecular_function | methionine adenosyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004478 | molecular_function | methionine adenosyltransferase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004478 | molecular_function | methionine adenosyltransferase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006556 | biological_process | S-adenosylmethionine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 501 |
| Chain | Residue |
| A | ASP32 |
| A | HOH630 |
| A | HOH640 |
| A | HOH783 |
| A | HOH784 |
| A | HOH787 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | GLN19 |
| A | ARG206 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | MET302 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | LYS26 |
| B | ASP32 |
| B | HOH615 |
| B | HOH628 |
| B | HOH777 |
| B | HOH779 |
| D | HOH796 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 502 |
| Chain | Residue |
| B | GLN19 |
| B | ARG206 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue MES C 501 |
| Chain | Residue |
| B | ARG174 |
| B | LYS245 |
| B | GLU246 |
| B | ILE247 |
| B | THR248 |
| B | SER249 |
| C | GLU9 |
| C | HIS366 |
| C | SER367 |
| C | HOH653 |
| C | HOH754 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MN C 502 |
| Chain | Residue |
| A | HOH792 |
| C | ASP32 |
| C | HOH625 |
| C | HOH637 |
| C | HOH776 |
| C | HOH781 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 503 |
| Chain | Residue |
| A | VAL11 |
| A | ARG12 |
| C | ARG12 |
| C | THR13 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue MES D 501 |
| Chain | Residue |
| A | ARG174 |
| A | LYS245 |
| A | GLU246 |
| A | ILE247 |
| A | THR248 |
| A | SER249 |
| D | GLU9 |
| D | HIS366 |
| D | SER367 |
| D | HOH634 |
| D | HOH770 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MN D 502 |
| Chain | Residue |
| B | HOH623 |
| B | HOH796 |
| D | ASP32 |
| D | HOH658 |
| D | HOH781 |
| D | HOH790 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00136 |
| Chain | Residue | Details |
| A | GLY136 | |
| B | GLY136 | |
| C | GLY136 | |
| D | GLY136 |
