4Q41
Crystal structure of Schistosoma mansoni arginase in complex with L-lysine
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 | 7 |
Details | BINDING SITE FOR RESIDUE MN A 401 |
Chain | Residue |
A | HIS131 |
A | ASP154 |
A | ASP158 |
A | ASP262 |
A | MN402 |
A | HOH654 |
A | HOH655 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN A 402 |
Chain | Residue |
A | ASP262 |
A | ASP264 |
A | MN401 |
A | LYS403 |
A | HOH654 |
A | ASP154 |
A | HIS156 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE LYS A 403 |
Chain | Residue |
A | ASP158 |
A | ASN160 |
A | SER167 |
A | HIS171 |
A | GLY172 |
A | ASP213 |
A | ASP264 |
A | THR276 |
A | MN402 |
A | HOH502 |
A | HOH545 |
A | HOH607 |
A | HOH609 |
A | HOH653 |
A | HOH654 |
A | HOH655 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | ASN32 |
A | TYR41 |
A | GLU73 |
A | HOH651 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | GLU76 |
A | ASP79 |
A | PRO80 |
A | GLN81 |
A | LYS86 |
A | TRP87 |
site_id | AC6 |
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 | HOH637 |
B | HOH638 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 402 |
Chain | Residue |
B | ASP154 |
B | HIS156 |
B | ASP262 |
B | ASP264 |
B | MN401 |
B | LYS403 |
B | HOH637 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS B 403 |
Chain | Residue |
B | HIS156 |
B | ASN160 |
B | SER167 |
B | HIS171 |
B | ASP213 |
B | ASP264 |
B | THR276 |
B | MN402 |
B | HOH533 |
B | HOH534 |
B | HOH535 |
B | HOH609 |
B | HOH637 |
B | HOH638 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | ASN32 |
B | ILE38 |
B | GLU73 |
B | HOH632 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 405 |
Chain | Residue |
B | ASP79 |
B | PRO80 |
B | GLN81 |
B | TRP87 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 401 |
Chain | Residue |
C | HIS131 |
C | ASP154 |
C | ASP158 |
C | ASP262 |
C | MN402 |
C | HOH545 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 402 |
Chain | Residue |
C | ASP154 |
C | HIS156 |
C | ASP262 |
C | ASP264 |
C | MN401 |
C | HOH545 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 403 |
Chain | Residue |
C | ASN32 |
C | ILE38 |
C | GLU73 |
C | HOH581 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 404 |
Chain | Residue |
C | ASP79 |
C | PRO80 |
C | GLN81 |
C | LYS86 |
C | TRP87 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 400 |
Chain | Residue |
D | ASP158 |
D | ASP262 |
D | MN401 |
D | HIS131 |
D | ASP154 |
site_id | BC7 |
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 | HOH522 |
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 |