2GWC
Crystal structure of plant glutamate cysteine ligase in complex with a transition state analogue
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004357 | molecular_function | glutamate-cysteine ligase activity |
A | 0006750 | biological_process | glutathione biosynthetic process |
A | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0004357 | molecular_function | glutamate-cysteine ligase activity |
B | 0006750 | biological_process | glutathione biosynthetic process |
B | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
C | 0003824 | molecular_function | catalytic activity |
C | 0004357 | molecular_function | glutamate-cysteine ligase activity |
C | 0006750 | biological_process | glutathione biosynthetic process |
C | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
D | 0003824 | molecular_function | catalytic activity |
D | 0004357 | molecular_function | glutamate-cysteine ligase activity |
D | 0006750 | biological_process | glutathione biosynthetic process |
D | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
E | 0003824 | molecular_function | catalytic activity |
E | 0004357 | molecular_function | glutamate-cysteine ligase activity |
E | 0006750 | biological_process | glutathione biosynthetic process |
E | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
F | 0003824 | molecular_function | catalytic activity |
F | 0004357 | molecular_function | glutamate-cysteine ligase activity |
F | 0006750 | biological_process | glutathione biosynthetic process |
F | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
G | 0003824 | molecular_function | catalytic activity |
G | 0004357 | molecular_function | glutamate-cysteine ligase activity |
G | 0006750 | biological_process | glutathione biosynthetic process |
G | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
H | 0003824 | molecular_function | catalytic activity |
H | 0004357 | molecular_function | glutamate-cysteine ligase activity |
H | 0006750 | biological_process | glutathione biosynthetic process |
H | 0042398 | biological_process | cellular modified amino acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1 |
Chain | Residue |
A | BSC2 |
A | GLU107 |
A | GLU159 |
A | GLU165 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG B 1 |
Chain | Residue |
B | BSC2 |
B | GLU107 |
B | GLU159 |
B | GLU165 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG C 1 |
Chain | Residue |
C | GLU107 |
C | GLU159 |
C | GLU165 |
C | BSC2 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG D 1 |
Chain | Residue |
D | BSC2 |
D | GLU107 |
D | GLU159 |
D | GLU165 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 1 |
Chain | Residue |
E | BSC2 |
E | GLU107 |
E | GLU159 |
E | GLU165 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG F 1 |
Chain | Residue |
F | BSC2 |
F | GLU107 |
F | GLU159 |
F | GLU165 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG G 1 |
Chain | Residue |
G | BSC2 |
G | GLU107 |
G | GLU159 |
G | GLU165 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG H 1 |
Chain | Residue |
H | BSC2 |
H | GLU107 |
H | GLU159 |
H | GLU165 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BSC A 2 |
Chain | Residue |
A | MG1 |
A | GLU107 |
A | GLU159 |
A | PRO160 |
A | THR242 |
A | CYS243 |
A | THR244 |
A | ARG292 |
A | TRP296 |
A | PHE375 |
A | ARG387 |
A | HOH571 |
site_id | BC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BSC B 2 |
Chain | Residue |
B | MG1 |
B | GLU107 |
B | GLU159 |
B | PRO160 |
B | MSE224 |
B | MSE238 |
B | THR242 |
B | CYS243 |
B | THR244 |
B | ARG292 |
B | TRP296 |
B | PHE375 |
B | ARG387 |
B | HOH560 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BSC C 2 |
Chain | Residue |
C | MG1 |
C | GLU107 |
C | GLU159 |
C | PRO160 |
C | MSE224 |
C | MSE238 |
C | THR242 |
C | CYS243 |
C | THR244 |
C | ARG292 |
C | TRP296 |
C | PHE375 |
C | ARG387 |
C | HOH531 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BSC D 2 |
Chain | Residue |
D | MG1 |
D | GLU107 |
D | GLU159 |
D | PRO160 |
D | MSE224 |
D | THR242 |
D | CYS243 |
D | THR244 |
D | ARG292 |
D | TRP296 |
D | PHE375 |
D | ARG387 |
D | HOH534 |
site_id | BC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE BSC E 2 |
Chain | Residue |
E | HOH586 |
E | MG1 |
E | GLU107 |
E | GLU159 |
E | PRO160 |
E | MSE224 |
E | MSE238 |
E | THR242 |
E | CYS243 |
E | THR244 |
E | ARG292 |
E | TRP296 |
E | PHE375 |
E | ARG387 |
E | HOH520 |
site_id | BC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BSC F 2 |
Chain | Residue |
F | MG1 |
F | GLU107 |
F | GLU159 |
F | PRO160 |
F | MSE224 |
F | THR242 |
F | CYS243 |
F | THR244 |
F | ARG292 |
F | TRP296 |
F | PHE375 |
F | ARG387 |
F | HOH542 |
site_id | BC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE BSC G 2 |
Chain | Residue |
G | MG1 |
G | GLU107 |
G | GLU159 |
G | PRO160 |
G | MSE224 |
G | THR242 |
G | CYS243 |
G | THR244 |
G | ARG292 |
G | TRP296 |
G | PHE375 |
G | ARG387 |
G | HOH549 |
G | HOH626 |
site_id | BC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BSC H 2 |
Chain | Residue |
H | MG1 |
H | GLU107 |
H | GLU159 |
H | MSE224 |
H | THR242 |
H | CYS243 |
H | THR244 |
H | ARG292 |
H | TRP296 |
H | PHE375 |
H | ARG387 |
H | HOH523 |