6DKT
Crystal structure of Arginase from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000050 | biological_process | urea cycle |
A | 0004053 | molecular_function | arginase activity |
A | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 |
E | 0000050 | biological_process | urea cycle |
E | 0004053 | molecular_function | arginase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006525 | biological_process | arginine metabolic process |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
E | 0030145 | molecular_function | manganese ion binding |
E | 0046872 | molecular_function | metal ion binding |
F | 0000050 | biological_process | urea cycle |
F | 0004053 | molecular_function | arginase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006525 | biological_process | arginine metabolic process |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
F | 0030145 | molecular_function | manganese ion binding |
F | 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 500 |
Chain | Residue |
A | HIS97 |
A | ASP120 |
A | ASP124 |
A | ASP223 |
A | MN501 |
A | HOH643 |
A | HOH659 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MN A 501 |
Chain | Residue |
A | ASP223 |
A | ASP225 |
A | MN500 |
A | HOH643 |
A | ASP120 |
A | HIS122 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MN B 500 |
Chain | Residue |
B | HIS97 |
B | TRP118 |
B | ASP120 |
B | ASP124 |
B | ASP223 |
B | MN501 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MN B 501 |
Chain | Residue |
B | ASP120 |
B | HIS122 |
B | ASP223 |
B | ASP225 |
B | MN500 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MN C 500 |
Chain | Residue |
C | HIS97 |
C | ASP120 |
C | ASP124 |
C | ASP223 |
C | MN501 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue MN C 501 |
Chain | Residue |
C | ASP120 |
C | HIS122 |
C | ASP223 |
C | ASP225 |
C | MN500 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue MN D 500 |
Chain | Residue |
D | HIS97 |
D | TRP118 |
D | ASP120 |
D | ASP124 |
D | ASP223 |
D | MN501 |
D | HOH688 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue MN D 501 |
Chain | Residue |
D | ASP120 |
D | HIS122 |
D | ASP223 |
D | ASP225 |
D | MN500 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MN E 500 |
Chain | Residue |
E | HIS97 |
E | TRP118 |
E | ASP120 |
E | ASP124 |
E | ASP223 |
E | MN501 |
E | HOH633 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MN E 501 |
Chain | Residue |
E | ASP120 |
E | HIS122 |
E | ASP223 |
E | ASP225 |
E | MN500 |
E | HOH633 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MN F 500 |
Chain | Residue |
F | HIS97 |
F | ASP120 |
F | ASP124 |
F | ASP223 |
F | MN501 |
F | HOH610 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue MN F 501 |
Chain | Residue |
F | ASP120 |
F | HIS122 |
F | ASP223 |
F | ASP225 |
F | MN500 |
F | HOH610 |
Functional Information from PROSITE/UniProt
site_id | PS01053 |
Number of Residues | 22 |
Details | ARGINASE_1 Arginase family signature. SLDLDgldPndaPGvgtpvvgG |
Chain | Residue | Details |
A | SER221-GLY242 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 52 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P53608","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |