3AEJ
Reaction intermediate structure of Entamoeba histolytica methionine gamma-lyase 1 tetramer containing Michaelis complex and methionine-pyridoxal-5'-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0018826 | molecular_function | methionine gamma-lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0018826 | molecular_function | methionine gamma-lyase activity |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0018826 | molecular_function | methionine gamma-lyase activity |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AA5 A 2001 |
| Chain | Residue |
| A | SER82 |
| A | LYS205 |
| A | GLY215 |
| A | SER332 |
| A | THR347 |
| A | ARG367 |
| D | TYR1553 |
| D | ARG1555 |
| A | GLY83 |
| A | MET84 |
| A | TYR108 |
| A | GLU151 |
| A | ASN155 |
| A | ASP180 |
| A | SER202 |
| A | SER204 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AA5 B 2002 |
| Chain | Residue |
| B | SER582 |
| B | GLY583 |
| B | MET584 |
| B | TYR608 |
| B | ASN655 |
| B | ASP680 |
| B | SER702 |
| B | SER704 |
| B | LYS705 |
| B | GLY715 |
| B | SER832 |
| B | THR847 |
| B | ARG867 |
| C | TYR1053 |
| C | ARG1055 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MET C 2003 |
| Chain | Residue |
| B | PHE544 |
| C | TYR1108 |
| C | ASN1155 |
| C | LLP1205 |
| C | SER1332 |
| C | LEU1333 |
| C | THR1347 |
| C | ARG1367 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE AA5 D 2004 |
| Chain | Residue |
| A | PHE44 |
| A | TYR53 |
| A | ARG55 |
| D | SER1582 |
| D | GLY1583 |
| D | MET1584 |
| D | TYR1608 |
| D | GLU1651 |
| D | ASN1655 |
| D | ASP1680 |
| D | PHE1683 |
| D | SER1702 |
| D | SER1704 |
| D | LYS1705 |
| D | GLY1715 |
| D | SER1832 |
| D | THR1847 |
| D | ARG1867 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2005 |
| Chain | Residue |
| A | ARG176 |
| A | HOH3237 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2006 |
| Chain | Residue |
| B | ARG676 |
| B | HOH3226 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2007 |
| Chain | Residue |
| C | ARG1176 |
| C | HOH3388 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 D 2008 |
| Chain | Residue |
| D | ARG1676 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 2009 |
| Chain | Residue |
| A | HOH3121 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL C 2010 |
| Chain | Residue |
| C | LYS1312 |
| C | HOH3018 |
| C | HOH3127 |
