6DKT
Crystal structure of Arginase from Bacillus subtilis
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 | 0006525 | biological_process | arginine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0030145 | molecular_function | manganese ion 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 | 0006525 | biological_process | arginine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000050 | biological_process | urea cycle |
| C | 0004053 | molecular_function | arginase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000050 | biological_process | urea cycle |
| D | 0004053 | molecular_function | arginase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006525 | biological_process | arginine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000050 | biological_process | urea cycle |
| E | 0004053 | molecular_function | arginase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006525 | biological_process | arginine metabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0030145 | molecular_function | manganese ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000050 | biological_process | urea cycle |
| F | 0004053 | molecular_function | arginase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006525 | biological_process | arginine metabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0030145 | molecular_function | manganese ion binding |
| F | 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 500 |
| Chain | Residue |
| A | HIS97 |
| A | ASP120 |
| A | ASP124 |
| A | ASP223 |
| A | MN501 |
| A | HOH643 |
| A | HOH659 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 501 |
| Chain | Residue |
| A | ASP223 |
| A | ASP225 |
| A | MN500 |
| A | HOH643 |
| A | ASP120 |
| A | HIS122 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 500 |
| Chain | Residue |
| B | HIS97 |
| B | TRP118 |
| B | ASP120 |
| B | ASP124 |
| B | ASP223 |
| B | MN501 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | ASP120 |
| B | HIS122 |
| B | ASP223 |
| B | ASP225 |
| B | MN500 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN C 500 |
| Chain | Residue |
| C | HIS97 |
| C | ASP120 |
| C | ASP124 |
| C | ASP223 |
| C | MN501 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MN C 501 |
| Chain | Residue |
| C | ASP120 |
| C | HIS122 |
| C | ASP223 |
| C | ASP225 |
| C | MN500 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue MN D 500 |
| Chain | Residue |
| D | HIS97 |
| D | TRP118 |
| D | ASP120 |
| D | ASP124 |
| D | ASP223 |
| D | MN501 |
| D | HOH688 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MN D 501 |
| Chain | Residue |
| D | ASP120 |
| D | HIS122 |
| D | ASP223 |
| D | ASP225 |
| D | MN500 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MN E 500 |
| Chain | Residue |
| E | HIS97 |
| E | TRP118 |
| E | ASP120 |
| E | ASP124 |
| E | ASP223 |
| E | MN501 |
| E | HOH633 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MN E 501 |
| Chain | Residue |
| E | ASP120 |
| E | HIS122 |
| E | ASP223 |
| E | ASP225 |
| E | MN500 |
| E | HOH633 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MN F 500 |
| Chain | Residue |
| F | HIS97 |
| F | ASP120 |
| F | ASP124 |
| F | ASP223 |
| F | MN501 |
| F | HOH610 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MN F 501 |
| Chain | Residue |
| F | ASP120 |
| F | HIS122 |
| F | ASP223 |
| F | ASP225 |
| F | MN500 |
| F | HOH610 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SLDLDgldPndaPGvgtpvvgG |
| Chain | Residue | Details |
| A | SER221-GLY242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






