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 | 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 | 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 |