Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000050 | biological_process | urea cycle |
A | 0004053 | molecular_function | arginase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006525 | biological_process | arginine metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019547 | biological_process | arginine catabolic process to ornithine |
A | 0030145 | molecular_function | manganese ion binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0000050 | biological_process | urea cycle |
B | 0004053 | molecular_function | arginase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006525 | biological_process | arginine metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0019547 | biological_process | arginine catabolic process to ornithine |
B | 0030145 | molecular_function | manganese ion binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue NVA A 301 |
Chain | Residue |
A | ASN130 |
A | SER137 |
A | HIS141 |
A | ASP178 |
A | HOH403 |
A | HOH413 |
A | HOH421 |
A | HOH463 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 302 |
Chain | Residue |
A | ASP124 |
A | ASP128 |
A | ASP225 |
A | MN303 |
A | HOH426 |
A | HIS98 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue MN A 303 |
Chain | Residue |
A | ASP124 |
A | HIS126 |
A | ASP225 |
A | ASP227 |
A | MN302 |
A | HOH426 |
A | HOH463 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | MET160 |
A | PRO161 |
A | HIS162 |
A | TYR163 |
A | HOH401 |
A | HOH460 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | ILE50 |
A | THR51 |
A | PRO53 |
A | SER72 |
A | VAL73 |
A | GLU76 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | VAL109 |
A | LYS110 |
A | MET112 |
B | SER158 |
B | EDO304 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue NVA B 301 |
Chain | Residue |
B | HIS126 |
B | ASN130 |
B | SER137 |
B | HIS141 |
B | ASP178 |
B | HOH410 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MN B 302 |
Chain | Residue |
B | HIS98 |
B | ASP124 |
B | ASP128 |
B | ASP225 |
B | MN303 |
B | HOH431 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MN B 303 |
Chain | Residue |
B | ASP124 |
B | HIS126 |
B | ASP225 |
B | ASP227 |
B | MN302 |
B | HOH431 |
B | HOH437 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | LYS110 |
A | ALA111 |
A | EDO306 |
B | ARG78 |
B | SER158 |
B | HOH419 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS98 | |
B | ASP128 | |
B | ASP225 | |
B | ASP227 | |
A | ASP124 | |
A | HIS126 | |
A | ASP128 | |
A | ASP225 | |
A | ASP227 | |
B | HIS98 | |
B | ASP124 | |
B | HIS126 | |
Chain | Residue | Details |
A | ASN130 | |
A | SER137 | |
A | ASP178 | |
A | THR239 | |
B | ASN130 | |
B | SER137 | |
B | ASP178 | |
B | THR239 | |