4Q40
Crystal structure of Schistosoma mansoni arginase in complex with L-valine
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 | 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 | 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 | 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 | 0030145 | molecular_function | manganese ion binding |
| D | 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 | HIS131 |
| A | ASP154 |
| A | ASP158 |
| A | ASP262 |
| A | MN402 |
| A | HOH579 |
| A | HOH581 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP262 |
| A | ASP264 |
| A | MN401 |
| A | HOH579 |
| A | ASP154 |
| A | HIS156 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE VAL A 403 |
| Chain | Residue |
| A | ASN160 |
| A | SER167 |
| A | GLY172 |
| A | ASP213 |
| A | HOH517 |
| A | HOH564 |
| A | HOH565 |
| A | HOH567 |
| A | HOH569 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASN32 |
| A | ILE38 |
| A | GLU73 |
| A | HOH663 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | ASP79 |
| A | PRO80 |
| A | GLN81 |
| A | LYS86 |
| A | TRP87 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 406 |
| Chain | Residue |
| A | ASP65 |
| A | CYS66 |
| A | GLY67 |
| A | HOH705 |
| C | GLN81 |
| C | ARG82 |
| C | PHE83 |
| C | GLY84 |
| C | IMD401 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 407 |
| Chain | Residue |
| A | ILE70 |
| A | PRO71 |
| A | GLU73 |
| A | HOH788 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IMD A 408 |
| Chain | Residue |
| A | GLU45 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| B | HIS131 |
| B | ASP154 |
| B | ASP158 |
| B | ASP262 |
| B | MN402 |
| B | HOH535 |
| B | HOH680 |
| site_id | BC1 |
| 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 | HOH680 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE VAL B 403 |
| Chain | Residue |
| B | ASP158 |
| B | ASN160 |
| B | SER167 |
| B | GLY172 |
| B | ASP213 |
| B | HOH531 |
| B | HOH579 |
| B | HOH581 |
| B | HOH590 |
| B | HOH595 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| B | ASN32 |
| B | GLU73 |
| B | HOH629 |
| B | HOH812 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | ASP79 |
| B | PRO80 |
| B | GLN81 |
| B | LYS86 |
| B | TRP87 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD B 406 |
| Chain | Residue |
| B | PRO71 |
| B | GLU73 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD B 407 |
| Chain | Residue |
| B | GLN81 |
| B | GLY84 |
| B | LYS86 |
| B | ALA166 |
| B | SER167 |
| B | HOH607 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IMD B 408 |
| Chain | Residue |
| B | TYR227 |
| B | PHE228 |
| B | ASP232 |
| B | HOH658 |
| B | HOH733 |
| B | HOH790 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IMD C 401 |
| Chain | Residue |
| A | ASP68 |
| A | ARG101 |
| A | GOL406 |
| A | HOH550 |
| A | HOH704 |
| C | LEU163 |
| C | GLN351 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN C 402 |
| Chain | Residue |
| C | ASP154 |
| C | ASP158 |
| C | ASP262 |
| C | MN403 |
| C | HOH546 |
| C | HOH547 |
| C | HIS131 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 403 |
| Chain | Residue |
| C | ASP154 |
| C | HIS156 |
| C | ASP262 |
| C | ASP264 |
| C | MN402 |
| C | HOH546 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE VAL C 404 |
| Chain | Residue |
| C | ASN160 |
| C | SER167 |
| C | GLY172 |
| C | ASP213 |
| C | HOH521 |
| C | HOH524 |
| C | HOH549 |
| C | HOH552 |
| C | HOH665 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 405 |
| Chain | Residue |
| C | ASN32 |
| C | ILE38 |
| C | GLU73 |
| C | HOH539 |
| C | HOH728 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 406 |
| Chain | Residue |
| C | ASP79 |
| C | PRO80 |
| C | GLN81 |
| C | LYS86 |
| C | TRP87 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IMD C 407 |
| Chain | Residue |
| C | GLN81 |
| C | GLY84 |
| C | LYS86 |
| C | ALA166 |
| C | SER167 |
| C | HOH669 |
| C | HOH702 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN D 401 |
| Chain | Residue |
| D | HIS131 |
| D | ASP154 |
| D | ASP158 |
| D | ASP262 |
| D | MN402 |
| D | HOH510 |
| D | HOH511 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN D 402 |
| Chain | Residue |
| D | ASP154 |
| D | HIS156 |
| D | ASP262 |
| D | ASP264 |
| D | MN401 |
| D | HOH510 |
| site_id | CC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE VAL D 403 |
| Chain | Residue |
| D | ASN160 |
| D | SER167 |
| D | GLY172 |
| D | ASP213 |
| D | HOH514 |
| D | HOH515 |
| D | HOH516 |
| D | HOH517 |
| D | HOH563 |
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 |
