3IJ6
CRYSTAL STRUCTURE OF AN UNCHARACTERIZED METAL-DEPENDENT HYDROLASE FROM Lactobacillus acidophilus
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019748 | biological_process | secondary metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019748 | biological_process | secondary metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016829 | molecular_function | lyase activity |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0019748 | biological_process | secondary metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016829 | molecular_function | lyase activity |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0019748 | biological_process | secondary metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 312 |
Chain | Residue |
A | HIS10 |
A | HIS160 |
A | HIS204 |
A | ASP262 |
A | HOH357 |
A | HOH358 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 313 |
Chain | Residue |
A | GLU304 |
A | ILE118 |
A | ASP121 |
A | LEU124 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 312 |
Chain | Residue |
B | HIS10 |
B | HIS160 |
B | HIS204 |
B | ASP262 |
B | HOH394 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 313 |
Chain | Residue |
B | ILE118 |
B | ASP121 |
B | LEU124 |
B | HOH354 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 312 |
Chain | Residue |
C | HIS10 |
C | HIS160 |
C | HIS204 |
C | ASP262 |
C | HOH329 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 313 |
Chain | Residue |
C | ILE118 |
C | ASP121 |
C | GLU122 |
C | LEU124 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 312 |
Chain | Residue |
D | HIS10 |
D | HIS160 |
D | HIS204 |
D | ASP262 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA D 313 |
Chain | Residue |
D | ILE118 |
D | ASP121 |
D | LEU124 |
D | HOH394 |