4Q3R
Crystal structure of Schistosoma mansoni arginase in complex with inhibitor ABHDP
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 | XA2407 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 402 |
Chain | Residue |
A | ASP264 |
A | MN401 |
A | XA2407 |
A | ASP154 |
A | HIS156 |
A | ASP262 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS A 403 |
Chain | Residue |
A | TYR227 |
A | ASP232 |
A | CL406 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS A 404 |
Chain | Residue |
A | GLY313 |
A | HOH737 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS A 405 |
Chain | Residue |
A | ARG48 |
A | LYS49 |
A | SER50 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 406 |
Chain | Residue |
A | TYR227 |
A | PHE228 |
A | CS403 |
A | HOH691 |
A | HOH735 |
site_id | AC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE XA2 A 407 |
Chain | Residue |
A | GLU58 |
A | HIS131 |
A | ASP154 |
A | HIS156 |
A | ASP158 |
A | ASN160 |
A | SER167 |
A | HIS171 |
A | ASP211 |
A | ASP213 |
A | ASP262 |
A | ASP264 |
A | THR276 |
A | GLU307 |
A | MN401 |
A | MN402 |
A | HOH536 |
A | HOH537 |
A | HOH553 |
A | HOH627 |
A | HOH630 |
A | HOH640 |
A | HOH655 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 408 |
Chain | Residue |
A | GLU76 |
A | ASP79 |
A | PRO80 |
A | GLN81 |
A | LYS86 |
A | TRP87 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 409 |
Chain | Residue |
A | ASN32 |
A | GLU73 |
A | HOH645 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PGE A 410 |
Chain | Residue |
A | ARG252 |
A | LEU253 |
A | GLU254 |
A | THR297 |
A | LYS299 |
B | ARG252 |
B | LEU253 |
B | GLU254 |
B | THR297 |
B | LYS299 |
site_id | BC2 |
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 | XA2409 |
site_id | BC3 |
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 | XA2409 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS B 403 |
Chain | Residue |
B | TYR227 |
B | ASP232 |
B | CL407 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS B 404 |
Chain | Residue |
B | LEU311 |
B | GLY313 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS B 405 |
Chain | Residue |
B | ARG48 |
B | SER50 |
B | CL408 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS B 406 |
Chain | Residue |
A | ASP350 |
B | ASP190 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 407 |
Chain | Residue |
B | TYR227 |
B | CS403 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 408 |
Chain | Residue |
B | LYS49 |
B | SER50 |
B | CS405 |
site_id | CC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE XA2 B 409 |
Chain | Residue |
B | ASN160 |
B | SER167 |
B | HIS171 |
B | ASP211 |
B | ASP213 |
B | ASP262 |
B | ASP264 |
B | THR276 |
B | GLU307 |
B | MN401 |
B | MN402 |
B | HOH512 |
B | HOH523 |
B | HOH540 |
B | HOH575 |
B | HOH628 |
B | GLU58 |
B | HIS131 |
B | ASP154 |
B | HIS156 |
B | ASP158 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 410 |
Chain | Residue |
B | ASP79 |
B | PRO80 |
B | GLN81 |
B | LYS86 |
B | TRP87 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 411 |
Chain | Residue |
B | ASN32 |
B | GLU73 |
B | HOH663 |
site_id | CC4 |
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 | XA2407 |
site_id | CC5 |
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 | XA2407 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS C 403 |
Chain | Residue |
C | TYR227 |
C | ASP232 |
C | CL405 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS C 404 |
Chain | Residue |
C | ARG48 |
C | LYS49 |
C | SER50 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 405 |
Chain | Residue |
C | TYR227 |
C | CS403 |
C | HOH550 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS C 406 |
Chain | Residue |
C | LEU311 |
C | GLY313 |
site_id | DC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE XA2 C 407 |
Chain | Residue |
C | GLU58 |
C | HIS131 |
C | ASP154 |
C | HIS156 |
C | ASP158 |
C | ASN160 |
C | SER167 |
C | HIS171 |
C | ASP211 |
C | ASP213 |
C | ASP262 |
C | ASP264 |
C | THR276 |
C | GLU307 |
C | MN401 |
C | MN402 |
C | HOH509 |
C | HOH511 |
C | HOH525 |
C | HOH538 |
site_id | DC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 408 |
Chain | Residue |
C | ASP79 |
C | PRO80 |
C | GLN81 |
C | LYS86 |
C | TRP87 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 409 |
Chain | Residue |
C | ASN32 |
C | ILE38 |
C | TYR41 |
C | GLU73 |
C | HOH563 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 401 |
Chain | Residue |
D | HIS131 |
D | ASP154 |
D | ASP158 |
D | ASP262 |
D | MN402 |
D | XA2404 |
site_id | DC5 |
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 | XA2404 |
site_id | DC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS D 403 |
Chain | Residue |
D | TYR227 |
D | ASP232 |
site_id | DC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE XA2 D 404 |
Chain | Residue |
D | HIS131 |
D | ASP154 |
D | HIS156 |
D | ASP158 |
D | ASN160 |
D | SER167 |
D | HIS171 |
D | GLY172 |
D | ASP211 |
D | ASP213 |
D | ASP262 |
D | ASP264 |
D | GLU307 |
D | MN401 |
D | MN402 |
D | HOH505 |
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 | |
C | SER260-GLY281 |