4MKJ
Crystal structure of L-methionine gamma-lyase from Citrobacter freundii modified by allicine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000096 | biological_process | sulfur amino acid metabolic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0018826 | molecular_function | methionine gamma-lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047982 | molecular_function | homocysteine desulfhydrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE A 401 |
| Chain | Residue |
| A | PRO191 |
| A | HOH713 |
| A | TYR192 |
| A | CYS193 |
| A | GLN195 |
| A | GLU266 |
| A | ARG304 |
| A | GLN305 |
| A | SER307 |
| A | HOH660 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE A 402 |
| Chain | Residue |
| A | GLU270 |
| A | LYS274 |
| A | PRO382 |
| A | GLU383 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 403 |
| Chain | Residue |
| A | ARG5 |
| A | ARG78 |
| A | GLU322 |
| A | ARG326 |
| A | HOH598 |
| A | HOH683 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 404 |
| Chain | Residue |
| A | THR116 |
| A | TYR154 |
| A | GLU156 |
| A | ASP185 |
