3PGA
STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 1 | 0004067 | molecular_function | asparaginase activity |
| 1 | 0004359 | molecular_function | glutaminase activity |
| 1 | 0006520 | biological_process | amino acid metabolic process |
| 1 | 0006528 | biological_process | asparagine metabolic process |
| 1 | 0016787 | molecular_function | hydrolase activity |
| 1 | 0042597 | cellular_component | periplasmic space |
| 1 | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| 2 | 0004067 | molecular_function | asparaginase activity |
| 2 | 0004359 | molecular_function | glutaminase activity |
| 2 | 0006520 | biological_process | amino acid metabolic process |
| 2 | 0006528 | biological_process | asparagine metabolic process |
| 2 | 0016787 | molecular_function | hydrolase activity |
| 2 | 0042597 | cellular_component | periplasmic space |
| 2 | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| 3 | 0004067 | molecular_function | asparaginase activity |
| 3 | 0004359 | molecular_function | glutaminase activity |
| 3 | 0006520 | biological_process | amino acid metabolic process |
| 3 | 0006528 | biological_process | asparagine metabolic process |
| 3 | 0016787 | molecular_function | hydrolase activity |
| 3 | 0042597 | cellular_component | periplasmic space |
| 3 | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| 4 | 0004067 | molecular_function | asparaginase activity |
| 4 | 0004359 | molecular_function | glutaminase activity |
| 4 | 0006520 | biological_process | amino acid metabolic process |
| 4 | 0006528 | biological_process | asparagine metabolic process |
| 4 | 0016787 | molecular_function | hydrolase activity |
| 4 | 0042597 | cellular_component | periplasmic space |
| 4 | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
Functional Information from PDB Data
| site_id | AS1 |
| Number of Residues | 7 |
| Details | active site COMPOSED OF SIDE CHAINS FROM THE N-TERMINAL DOMAIN OF CHAIN 1 AND THE C-TERMINAL DOMAIN OF CHAIN 3 |
| Chain | Residue |
| 1 | THR100 |
| 1 | LYS173 |
| 1 | ASP101 |
| 1 | TYR34 |
| 1 | THR20 |
| 3 | GLU294 |
| 3 | SER258 |
| site_id | AS2 |
| Number of Residues | 7 |
| Details | active site COMPOSED OF SIDE CHAINS FROM THE N-TERMINAL DOMAIN OF CHAIN 2 AND THE C-TERMINAL DOMAIN OF CHAIN 4 |
| Chain | Residue |
| 2 | ASP101 |
| 2 | TYR34 |
| 2 | THR20 |
| 4 | GLU294 |
| 4 | SER258 |
| 2 | THR100 |
| 2 | LYS173 |
| site_id | AS3 |
| Number of Residues | 7 |
| Details | active site COMPOSED OF SIDE CHAINS FROM THE N-TERMINAL DOMAIN OF CHAIN 3 AND THE C-TERMINAL DOMAIN OF CHAIN 1 |
| Chain | Residue |
| 3 | THR100 |
| 3 | LYS173 |
| 3 | ASP101 |
| 3 | TYR34 |
| 3 | THR20 |
| 1 | GLU294 |
| 1 | SER258 |
| site_id | AS4 |
| Number of Residues | 7 |
| Details | active site COMPOSED OF SIDE CHAINS FROM THE N-TERMINAL DOMAIN OF CHAIN 4 AND THE C-TERMINAL DOMAIN OF CHAIN 2 |
| Chain | Residue |
| 4 | THR100 |
| 4 | LYS173 |
| 4 | ASP101 |
| 4 | TYR34 |
| 4 | THR20 |
| 2 | GLU294 |
| 2 | SER258 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:10684596 |
| Chain | Residue | Details |
| 1 | THR20 | |
| 2 | THR20 | |
| 3 | THR20 | |
| 4 | THR20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| 1 | SER67 | |
| 1 | THR100 | |
| 2 | SER67 | |
| 2 | THR100 | |
| 3 | SER67 | |
| 3 | THR100 | |
| 4 | SER67 | |
| 4 | THR100 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| 1 | TYR34 | |
| 1 | THR100 | |
| 1 | THR20 | |
| 3 | GLU294 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| 4 | GLU294 | |
| 2 | TYR34 | |
| 2 | THR100 | |
| 2 | THR20 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| 1 | GLU294 | |
| 3 | TYR34 | |
| 3 | THR100 | |
| 3 | THR20 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1djo |
| Chain | Residue | Details |
| 4 | TYR34 | |
| 4 | THR100 | |
| 4 | THR20 | |
| 2 | GLU294 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| 1 | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| 1 | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| 1 | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| 1 | ASP101 | hydrogen bond acceptor |
| 1 | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| 1 | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| 2 | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| 2 | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| 2 | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| 2 | ASP101 | hydrogen bond acceptor |
| 2 | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| 2 | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| 3 | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| 3 | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| 3 | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| 3 | ASP101 | hydrogen bond acceptor |
| 3 | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| 3 | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 29 |
| Chain | Residue | Details |
| 4 | THR20 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| 4 | TYR34 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| 4 | THR100 | hydrogen bond acceptor, hydrogen bond donor |
| 4 | ASP101 | hydrogen bond acceptor |
| 4 | LYS173 | hydrogen bond acceptor, hydrogen bond donor |
| 4 | GLU294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
