1DJO
Crystal structure of Pseudomonas 7A Glutaminase-asparaginase with the inhibitor donv covalently bound in the active site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004067 | molecular_function | asparaginase activity |
A | 0004359 | molecular_function | glutaminase activity |
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 | 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 | 12 |
Details | BINDING SITE FOR RESIDUE CAB B 4000 |
Chain | Residue |
A | GLU1294 |
B | THR3100 |
B | ASP3101 |
B | SER3125 |
B | GLY3019 |
B | THR3020 |
B | TYR3034 |
B | ALA3036 |
B | ALA3066 |
B | SER3067 |
B | GLU3068 |
B | GLY3099 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CAB A 4001 |
Chain | Residue |
A | GLY1019 |
A | THR1020 |
A | TYR1034 |
A | ALA1066 |
A | SER1067 |
A | GLU1068 |
A | GLY1099 |
A | THR1100 |
A | ASP1101 |
A | SER1125 |
B | GLU3294 |
Functional Information from PROSITE/UniProt
site_id | PS00144 |
Number of Residues | 9 |
Details | ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA |
Chain | Residue | Details |
A | ILE1014-ALA1022 |
site_id | PS00917 |
Number of Residues | 11 |
Details | ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiVitHGTDTL |
Chain | Residue | Details |
A | GLY1093-LEU1103 |
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 | THR1020 | |
B | THR3020 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER1067 | |
A | THR1100 | |
B | SER3067 | |
B | THR3100 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 10684596 |
Chain | Residue | Details |
A | THR1020 | |
A | TYR1034 | |
A | THR1100 | |
B | GLU3294 |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 10684596 |
Chain | Residue | Details |
A | GLU1294 | |
B | THR3020 | |
B | THR3100 | |
B | TYR3034 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 29 |
Chain | Residue | Details |
A | THR1020 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | TYR1034 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | THR1100 | hydrogen bond acceptor, hydrogen bond donor |
A | ASP1101 | hydrogen bond acceptor |
A | LYS1173 | hydrogen bond acceptor, hydrogen bond donor |
A | GLU1294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 29 |
Chain | Residue | Details |
B | THR3020 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | TYR3034 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | THR3100 | hydrogen bond acceptor, hydrogen bond donor |
B | ASP3101 | hydrogen bond acceptor |
B | LYS3173 | hydrogen bond acceptor, hydrogen bond donor |
B | GLU3294 | hydrogen bond acceptor, proton acceptor, proton donor, proton relay |