5CEV
ARGINASE FROM BACILLUS CALDEVELOX, L-LYSINE COMPLEX
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 | 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 | 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 | 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 | 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 | 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 | 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 | 6 |
Details | BINDING SITE FOR RESIDUE MN A 300 |
Chain | Residue |
A | HIS99 |
A | ASP122 |
A | ASP126 |
A | ASP226 |
A | MN301 |
A | HOH407 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 301 |
Chain | Residue |
A | ASP122 |
A | HIS124 |
A | ASP226 |
A | ASP228 |
A | MN300 |
A | HOH407 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 300 |
Chain | Residue |
A | HOH408 |
B | HIS99 |
B | ASP122 |
B | ASP126 |
B | ASP226 |
B | MN301 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 301 |
Chain | Residue |
A | HOH408 |
B | ASP122 |
B | HIS124 |
B | ASP226 |
B | ASP228 |
B | MN300 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 300 |
Chain | Residue |
A | HOH409 |
C | HIS99 |
C | ASP122 |
C | ASP126 |
C | ASP226 |
C | MN301 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 301 |
Chain | Residue |
A | HOH409 |
C | ASP122 |
C | HIS124 |
C | ASP226 |
C | ASP228 |
C | MN300 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 300 |
Chain | Residue |
A | HOH410 |
D | HIS99 |
D | ASP122 |
D | ASP126 |
D | ASP226 |
D | MN301 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN D 301 |
Chain | Residue |
A | HOH410 |
D | ASP122 |
D | HIS124 |
D | ASP226 |
D | ASP228 |
D | MN300 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 300 |
Chain | Residue |
E | ASP126 |
E | ASP226 |
E | MN301 |
A | HOH411 |
E | HIS99 |
E | ASP122 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN E 301 |
Chain | Residue |
A | HOH411 |
E | ASP122 |
E | HIS124 |
E | ASP226 |
E | ASP228 |
E | MN300 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 300 |
Chain | Residue |
F | HIS99 |
F | ASP122 |
F | ASP126 |
F | ASP226 |
F | MN301 |
F | HOH302 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN F 301 |
Chain | Residue |
F | ASP122 |
F | HIS124 |
F | ASP226 |
F | ASP228 |
F | MN300 |
F | HOH302 |
site_id | BC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LYS A 401 |
Chain | Residue |
A | ASP126 |
A | ASN128 |
A | SER135 |
A | HIS139 |
A | ASP178 |
A | THR240 |
A | GLU271 |
A | HOH407 |
A | HOH413 |
A | HOH415 |
A | HOH435 |
A | HOH437 |
A | HOH480 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE LYS B 402 |
Chain | Residue |
A | HOH408 |
A | HOH427 |
A | HOH454 |
B | ASP126 |
B | ASN128 |
B | SER135 |
B | HIS139 |
B | ASP178 |
B | THR240 |
B | GLU271 |
B | HOH416 |
B | HOH428 |
site_id | BC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS C 403 |
Chain | Residue |
A | HOH409 |
A | HOH428 |
A | HOH455 |
A | HOH456 |
C | ASP126 |
C | ASN128 |
C | SER135 |
C | HIS139 |
C | ASP178 |
C | GLU181 |
C | THR240 |
C | GLU271 |
C | HOH418 |
C | HOH468 |
site_id | BC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS D 404 |
Chain | Residue |
A | HOH410 |
A | HOH434 |
A | HOH457 |
A | HOH458 |
D | ASP126 |
D | ASN128 |
D | SER135 |
D | HIS139 |
D | ASP178 |
D | GLU181 |
D | THR240 |
D | GLU271 |
D | HOH414 |
D | HOH469 |
site_id | BC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE LYS E 405 |
Chain | Residue |
A | HOH411 |
E | ASP126 |
E | ASN128 |
E | SER135 |
E | HIS139 |
E | ASP178 |
E | GLU181 |
E | THR240 |
E | GLU271 |
E | HOH418 |
E | HOH420 |
E | HOH436 |
E | HOH438 |
site_id | BC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE LYS F 406 |
Chain | Residue |
F | ASP126 |
F | ASN128 |
F | SER135 |
F | HIS139 |
F | GLY140 |
F | ASP178 |
F | GLU181 |
F | THR240 |
F | GLU271 |
F | HOH302 |
F | HOH307 |
F | HOH320 |
F | HOH322 |
F | HOH357 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI B 407 |
Chain | Residue |
A | HIS252 |
A | GLU256 |
B | MET195 |
B | HIS196 |
B | ASP199 |
B | HOH409 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI B 408 |
Chain | Residue |
B | HIS252 |
B | GLU256 |
C | MET195 |
C | HIS196 |
C | ASP199 |
C | HOH410 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI C 409 |
Chain | Residue |
A | HIS196 |
A | ASP199 |
A | HOH429 |
C | HIS252 |
C | GLU256 |
C | LEU298 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GAI E 410 |
Chain | Residue |
D | HIS252 |
D | LEU253 |
D | GLU256 |
E | ASP199 |
E | HOH412 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GAI F 411 |
Chain | Residue |
E | HIS252 |
E | GLU256 |
F | MET195 |
F | HIS196 |
F | ASP199 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GAI D 412 |
Chain | Residue |
D | ASP199 |
D | HOH427 |
F | ARG249 |
F | HIS252 |
F | LEU253 |
F | GLU256 |
site_id | MNA |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE A 300 AND A 301 MN A 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 1. MN A 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 1 |
Chain | Residue |
A | MN300 |
A | MN301 |
A | HIS99 |
A | ASP122 |
A | HIS124 |
A | ASP126 |
A | ASP226 |
A | ASP228 |
site_id | MNB |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE B 300 AND B 301 MN B 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 2. MN B 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 2 |
Chain | Residue |
B | MN301 |
B | HIS99 |
B | ASP122 |
B | HIS124 |
B | ASP126 |
B | ASP226 |
B | ASP228 |
B | MN300 |
site_id | MNC |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE C 300 AND C 301 MN C 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 3. MN C 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 3 |
Chain | Residue |
C | MN300 |
C | MN301 |
C | HIS99 |
C | ASP122 |
C | HIS124 |
C | ASP126 |
C | ASP226 |
C | ASP228 |
site_id | MND |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE D 300 AND D 301 MN D 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 4. MN D 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 4 |
Chain | Residue |
D | MN300 |
D | MN301 |
D | HIS99 |
D | ASP122 |
D | HIS124 |
D | ASP126 |
D | ASP226 |
D | ASP228 |
site_id | MNE |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE E 300 AND E 301 MN E 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 5. MN E 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 5 |
Chain | Residue |
E | MN300 |
E | MN301 |
E | HIS99 |
E | ASP122 |
E | HIS124 |
E | ASP126 |
E | ASP226 |
E | ASP228 |
site_id | MNF |
Number of Residues | 8 |
Details | SITE COMPRISES TWO MN ATOMS, RESIDUE F 300 AND F 301 MN F 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, AND A BRIDGING WATER HOH 6. MN F 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, ASP 228 OD2 AND THE BRIDGING WATER HOH 6 |
Chain | Residue |
F | MN300 |
F | MN301 |
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 |