2CEV
ARGINASE FROM BACILLUS CALDEVELOX, NATIVE STRUCTURE AT PH 8.5
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 | 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 | 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 | 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 | 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 |
E | 0000050 | biological_process | urea cycle |
E | 0004053 | molecular_function | arginase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
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 | 0019547 | biological_process | arginine catabolic process to ornithine |
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 | 0005829 | cellular_component | cytosol |
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 | 0019547 | biological_process | arginine catabolic process to ornithine |
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 301 |
Chain | Residue |
A | HIS99 |
A | ASP122 |
A | ASP126 |
A | ASP226 |
A | MN302 |
A | HOH1004 |
A | HOH1005 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 302 |
Chain | Residue |
A | ASP122 |
A | HIS124 |
A | ASP226 |
A | ASP228 |
A | MN301 |
A | HOH1004 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 301 |
Chain | Residue |
B | HIS99 |
B | ASP122 |
B | ASP126 |
B | ASP226 |
B | MN302 |
B | HOH1003 |
B | HOH1004 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 302 |
Chain | Residue |
B | ASP122 |
B | HIS124 |
B | ASP226 |
B | ASP228 |
B | MN301 |
B | HOH1003 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN C 301 |
Chain | Residue |
C | HIS99 |
C | ASP122 |
C | ASP126 |
C | ASP226 |
C | MN302 |
C | HOH303 |
C | HOH304 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 302 |
Chain | Residue |
C | ASP122 |
C | HIS124 |
C | ASP226 |
C | ASP228 |
C | MN301 |
C | HOH303 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN D 301 |
Chain | Residue |
D | HIS99 |
D | ASP122 |
D | ASP126 |
D | ASP226 |
D | MN302 |
D | HOH1005 |
D | HOH1006 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 302 |
Chain | Residue |
D | ASP122 |
D | HIS124 |
D | ASP226 |
D | ASP228 |
D | MN301 |
D | HOH1005 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN E 301 |
Chain | Residue |
E | HIS99 |
E | ASP122 |
E | ASP126 |
E | ASP226 |
E | MN302 |
E | HOH1006 |
E | HOH1007 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 302 |
Chain | Residue |
E | MN301 |
E | HOH1006 |
E | ASP122 |
E | HIS124 |
E | ASP226 |
E | ASP228 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN F 301 |
Chain | Residue |
F | HIS99 |
F | ASP122 |
F | ASP126 |
F | ASP226 |
F | MN302 |
F | HOH1007 |
F | HOH1008 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 302 |
Chain | Residue |
F | ASP122 |
F | HIS124 |
F | ASP226 |
F | ASP228 |
F | MN301 |
F | HOH1007 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GAI A 1001 |
Chain | Residue |
A | HIS252 |
A | GLU256 |
A | LEU298 |
A | HOH1070 |
B | HIS196 |
B | ASP199 |
B | HOH1005 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GAI B 1002 |
Chain | Residue |
B | HIS252 |
B | GLU256 |
C | HIS196 |
C | ASP199 |
C | HOH307 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GAI A 1003 |
Chain | Residue |
A | HIS196 |
A | ASP199 |
A | HOH1033 |
A | HOH1073 |
C | HIS252 |
C | GLU256 |
C | LEU298 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI D 1004 |
Chain | Residue |
D | HIS252 |
D | LEU253 |
D | GLU256 |
D | HOH1069 |
E | ASP199 |
E | HOH1008 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GAI E 1005 |
Chain | Residue |
E | HIS252 |
E | GLU256 |
E | LEU298 |
E | HOH1072 |
F | MET195 |
F | HIS196 |
F | ASP199 |
F | HOH1013 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GAI F 1006 |
Chain | Residue |
D | HIS196 |
D | ASP199 |
F | HIS252 |
F | GLU256 |
F | HOH1076 |
site_id | MNA |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH1 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH1 |
Chain | Residue |
A | HIS99 |
A | ASP122 |
A | HIS124 |
A | ASP126 |
A | ASP226 |
A | ASP228 |
site_id | MNB |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH2 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH2 |
Chain | Residue |
B | ASP126 |
B | ASP226 |
B | ASP228 |
B | HIS99 |
B | ASP122 |
B | HIS124 |
site_id | MNC |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH3 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH3 |
Chain | Residue |
C | HIS99 |
C | ASP122 |
C | HIS124 |
C | ASP126 |
C | ASP226 |
C | ASP228 |
site_id | MND |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH4 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH4 |
Chain | Residue |
D | HIS99 |
D | ASP122 |
D | HIS124 |
D | ASP126 |
D | ASP226 |
D | ASP228 |
site_id | MNE |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH5 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH5 |
Chain | Residue |
E | HIS99 |
E | ASP122 |
E | HIS124 |
E | ASP126 |
E | ASP226 |
E | ASP228 |
site_id | MNF |
Number of Residues | 6 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUES 301 AND 302. MN 301 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, A BRIDGING WATER HOH6 AND A TERMINAL WATER HOH MN 302 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH6 |
Chain | Residue |
F | HIS99 |
F | ASP122 |
F | HIS124 |
F | ASP126 |
F | ASP226 |
F | ASP228 |
Functional Information from PROSITE/UniProt
site_id | PS01053 |
Number of Residues | 22 |
Details | ARGINASE_1 Arginase family signature. SLDLDgldPsdaPGvgtpvigG |
Chain | Residue | Details |
A | SER224-GLY245 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10196128, ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV, ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV |
Chain | Residue | Details |
A | HIS99 | |
E | ASP126 | |
F | HIS99 | |
F | ASP126 | |
A | ASP126 | |
B | HIS99 | |
B | ASP126 | |
C | HIS99 | |
C | ASP126 | |
D | HIS99 | |
D | ASP126 | |
E | HIS99 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10196128, ECO:0007744|PDB:1CEV, ECO:0007744|PDB:2CEV, ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV |
Chain | Residue | Details |
A | ASP122 | |
C | HIS124 | |
C | ASP226 | |
C | ASP228 | |
D | ASP122 | |
D | HIS124 | |
D | ASP226 | |
D | ASP228 | |
E | ASP122 | |
E | HIS124 | |
E | ASP226 | |
A | HIS124 | |
E | ASP228 | |
F | ASP122 | |
F | HIS124 | |
F | ASP226 | |
F | ASP228 | |
A | ASP226 | |
A | ASP228 | |
B | ASP122 | |
B | HIS124 | |
B | ASP226 | |
B | ASP228 | |
C | ASP122 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10196128, ECO:0007744|PDB:3CEV, ECO:0007744|PDB:4CEV, ECO:0007744|PDB:5CEV |
Chain | Residue | Details |
A | SER135 | |
E | ASP178 | |
F | SER135 | |
F | ASP178 | |
A | ASP178 | |
B | SER135 | |
B | ASP178 | |
C | SER135 | |
C | ASP178 | |
D | SER135 | |
D | ASP178 | |
E | SER135 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10196128, ECO:0007744|PDB:3CEV |
Chain | Residue | Details |
A | THR240 | |
B | THR240 | |
C | THR240 | |
D | THR240 | |
E | THR240 | |
F | THR240 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10196128, ECO:0007744|PDB:3CEV, ECO:0007744|PDB:5CEV |
Chain | Residue | Details |
A | GLU271 | |
B | GLU271 | |
C | GLU271 | |
D | GLU271 | |
E | GLU271 | |
F | GLU271 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
A | ASP126 | |
A | GLU271 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
B | ASP126 | |
B | GLU271 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
C | ASP126 | |
C | GLU271 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
D | ASP126 | |
D | GLU271 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
E | ASP126 | |
E | GLU271 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1cev |
Chain | Residue | Details |
F | ASP126 | |
F | GLU271 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
A | HIS99 | metal ligand |
A | ASP122 | metal ligand |
A | HIS124 | metal ligand |
A | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
A | HIS139 | proton shuttle (general acid/base), steric role |
A | ASP226 | metal ligand |
A | ASP228 | metal ligand |
A | GLU271 | electrostatic stabiliser, steric role |
site_id | MCSA2 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
B | HIS99 | metal ligand |
B | ASP122 | metal ligand |
B | HIS124 | metal ligand |
B | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
B | HIS139 | proton shuttle (general acid/base), steric role |
B | ASP226 | metal ligand |
B | ASP228 | metal ligand |
B | GLU271 | electrostatic stabiliser, steric role |
site_id | MCSA3 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
C | HIS99 | metal ligand |
C | ASP122 | metal ligand |
C | HIS124 | metal ligand |
C | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
C | HIS139 | proton shuttle (general acid/base), steric role |
C | ASP226 | metal ligand |
C | ASP228 | metal ligand |
C | GLU271 | electrostatic stabiliser, steric role |
site_id | MCSA4 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
D | HIS99 | metal ligand |
D | ASP122 | metal ligand |
D | HIS124 | metal ligand |
D | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
D | HIS139 | proton shuttle (general acid/base), steric role |
D | ASP226 | metal ligand |
D | ASP228 | metal ligand |
D | GLU271 | electrostatic stabiliser, steric role |
site_id | MCSA5 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
E | HIS99 | metal ligand |
E | ASP122 | metal ligand |
E | HIS124 | metal ligand |
E | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
E | HIS139 | proton shuttle (general acid/base), steric role |
E | ASP226 | metal ligand |
E | ASP228 | metal ligand |
E | GLU271 | electrostatic stabiliser, steric role |
site_id | MCSA6 |
Number of Residues | 8 |
Details | M-CSA 445 |
Chain | Residue | Details |
F | HIS99 | metal ligand |
F | ASP122 | metal ligand |
F | HIS124 | metal ligand |
F | ASP126 | metal ligand, modifies pKa, proton shuttle (general acid/base) |
F | HIS139 | proton shuttle (general acid/base), steric role |
F | ASP226 | metal ligand |
F | ASP228 | metal ligand |
F | GLU271 | electrostatic stabiliser, steric role |