4PGA
GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 338 |
| Chain | Residue |
| A | GLY19 |
| A | THR20 |
| A | ALA66 |
| A | SER67 |
| A | GLY99 |
| A | THR100 |
| A | ASP101 |
| A | NH4339 |
| A | HOH435 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NH4 A 339 |
| Chain | Residue |
| A | GLU68 |
| A | ASP101 |
| A | SO4338 |
| B | SER258 |
| B | GLU294 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 338 |
| Chain | Residue |
| B | GLY19 |
| B | THR20 |
| B | ALA66 |
| B | SER67 |
| B | GLY99 |
| B | THR100 |
| B | ASP101 |
| B | NH4339 |
| B | HOH466 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NH4 B 339 |
| Chain | Residue |
| A | SER258 |
| A | GLU294 |
| B | GLU68 |
| B | ASP101 |
| B | SO4338 |
| site_id | AS1 |
| Number of Residues | 5 |
| Details | DESCRIPTION NOT PROVIDED |
| Chain | Residue |
| A | THR100 |
| A | LYS173 |
| A | ASP101 |
| A | TYR34 |
| A | THR20 |
| site_id | AS2 |
| Number of Residues | 5 |
| Details | DESCRIPTION NOT PROVIDED |
| Chain | Residue |
| B | THR20 |
| B | THR100 |
| B | LYS173 |
| B | ASP101 |
| B | TYR34 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:10684596 |
| Chain | Residue | Details |
| A | THR20 | |
| B | THR20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER67 | |
| A | THR100 | |
| B | SER67 | |
| B | THR100 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| A | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| A | ASP101 | hydrogen bond acceptor |
| A | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| A | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| B | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| B | ASP101 | hydrogen bond acceptor |
| B | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| B | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
