4Q3V
Crystal structure of Schistosoma mansoni arginase in complex with inhibitor BEC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000050 | biological_process | urea cycle |
| A | 0004053 | molecular_function | arginase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
| 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 | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
| 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 | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
| 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 | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| 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 | 0019547 | biological_process | arginine catabolic process to ornithine |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | HIS131 |
| A | ASP154 |
| A | ASP158 |
| A | ASP262 |
| A | MN402 |
| A | S2C405 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP264 |
| A | MN401 |
| A | S2C405 |
| A | ASP154 |
| A | HIS156 |
| A | ASP262 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | ASP79 |
| A | GLN81 |
| A | LYS86 |
| A | TRP87 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASN32 |
| A | GLU73 |
| A | HOH540 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S2C A 405 |
| Chain | Residue |
| A | HIS131 |
| A | ASP154 |
| A | HIS156 |
| A | ASP158 |
| A | ASN160 |
| A | SER167 |
| A | HIS171 |
| A | ASP213 |
| A | ASP262 |
| A | ASP264 |
| A | THR276 |
| A | GLU307 |
| A | MN401 |
| A | MN402 |
| A | HOH538 |
| A | HOH609 |
| A | HOH624 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| B | HIS131 |
| B | ASP154 |
| B | ASP158 |
| B | ASP262 |
| B | MN402 |
| B | S2C405 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 402 |
| Chain | Residue |
| B | ASP154 |
| B | HIS156 |
| B | ASP262 |
| B | ASP264 |
| B | MN401 |
| B | S2C405 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | ASP79 |
| B | LYS86 |
| B | TRP87 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | ASN32 |
| B | TYR41 |
| B | GLU73 |
| B | HOH609 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE S2C B 405 |
| Chain | Residue |
| B | HIS131 |
| B | ASP154 |
| B | HIS156 |
| B | ASP158 |
| B | ASN160 |
| B | SER167 |
| B | HIS171 |
| B | ASP213 |
| B | ASP262 |
| B | ASP264 |
| B | THR276 |
| B | GLU307 |
| B | MN401 |
| B | MN402 |
| B | HOH528 |
| B | HOH532 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 401 |
| Chain | Residue |
| C | ASP154 |
| C | HIS156 |
| C | ASP262 |
| C | ASP264 |
| C | MN402 |
| C | S2C405 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 402 |
| Chain | Residue |
| C | HIS131 |
| C | ASP154 |
| C | ASP158 |
| C | ASP262 |
| C | MN401 |
| C | S2C405 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| C | GLU76 |
| C | ASP79 |
| C | PRO80 |
| C | GLN81 |
| C | LYS86 |
| C | TRP87 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 404 |
| Chain | Residue |
| C | ASN32 |
| C | ILE38 |
| C | GLU73 |
| C | HOH565 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE S2C C 405 |
| Chain | Residue |
| C | HIS171 |
| C | ASP213 |
| C | ASP262 |
| C | ASP264 |
| C | THR276 |
| C | GLU307 |
| C | MN401 |
| C | MN402 |
| C | HOH535 |
| C | HIS131 |
| C | ASP154 |
| C | HIS156 |
| C | ASP158 |
| C | ASN160 |
| C | SER167 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 400 |
| Chain | Residue |
| D | HIS131 |
| D | ASP154 |
| D | ASP158 |
| D | ASP262 |
| D | MN401 |
| D | HOH502 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 401 |
| Chain | Residue |
| D | ASP154 |
| D | HIS156 |
| D | ASP262 |
| D | ASP264 |
| D | MN400 |
| D | HOH502 |
Functional Information from PROSITE/UniProt
| site_id | PS01053 |
| Number of Residues | 22 |
| Details | ARGINASE_1 Arginase family signature. SFDIDaldPlvaPStgtavpgG |
| Chain | Residue | Details |
| A | SER260-GLY281 |
