6LUG
Crystal structure of N(omega)-hydroxy-L-arginine hydrolase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004053 | molecular_function | arginase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0019547 | biological_process | arginine catabolic process to ornithine |
A | 0030145 | molecular_function | manganese ion binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004053 | molecular_function | arginase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
B | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0019547 | biological_process | arginine catabolic process to ornithine |
B | 0030145 | molecular_function | manganese ion binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue MN A 401 |
Chain | Residue |
A | CYS86 |
A | ASP109 |
A | ASP113 |
A | ASP198 |
A | MN402 |
A | HOH523 |
A | HOH640 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 402 |
Chain | Residue |
A | ASP198 |
A | ASP200 |
A | MN401 |
A | HOH523 |
A | ASP109 |
A | HIS111 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MN B 401 |
Chain | Residue |
B | CYS86 |
B | ASP109 |
B | ASP113 |
B | ASP198 |
B | MN402 |
B | HOH540 |
B | HOH616 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MN B 402 |
Chain | Residue |
B | ASP109 |
B | HIS111 |
B | ASP198 |
B | ASP200 |
B | MN401 |
B | HOH540 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00742 |
Chain | Residue | Details |
A | ASP109 | |
B | ASP200 | |
A | HIS111 | |
A | ASP113 | |
A | ASP198 | |
A | ASP200 | |
B | ASP109 | |
B | HIS111 | |
B | ASP113 | |
B | ASP198 |