3ECA
CRYSTAL STRUCTURE OF ESCHERICHIA COLI L-ASPARAGINASE, AN ENZYME USED IN CANCER THERAPY (ELSPAR)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0006530 | biological_process | asparagine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0006530 | biological_process | asparagine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006528 | biological_process | asparagine metabolic process |
| C | 0006530 | biological_process | asparagine catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006528 | biological_process | asparagine metabolic process |
| D | 0006530 | biological_process | asparagine catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ASP A 401 |
| Chain | Residue |
| A | GLY11 |
| A | ALA114 |
| A | HOH539 |
| C | ASN248 |
| C | GLU283 |
| A | THR12 |
| A | TYR25 |
| A | GLY57 |
| A | SER58 |
| A | GLN59 |
| A | GLY88 |
| A | THR89 |
| A | ASP90 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ASP B 401 |
| Chain | Residue |
| B | GLY11 |
| B | THR12 |
| B | ALA27 |
| B | GLY57 |
| B | SER58 |
| B | GLN59 |
| B | GLY88 |
| B | THR89 |
| B | ASP90 |
| B | ALA114 |
| B | HOH558 |
| D | ASN248 |
| D | GLU283 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ASP C 401 |
| Chain | Residue |
| A | ASN248 |
| A | GLU283 |
| C | GLY11 |
| C | THR12 |
| C | ALA27 |
| C | GLY57 |
| C | SER58 |
| C | GLN59 |
| C | GLY88 |
| C | THR89 |
| C | ASP90 |
| C | ALA114 |
| C | HOH543 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue ASP D 401 |
| Chain | Residue |
| B | ASN248 |
| B | GLU283 |
| D | GLY11 |
| D | THR12 |
| D | ALA27 |
| D | GLY57 |
| D | SER58 |
| D | GLN59 |
| D | GLY88 |
| D | THR89 |
| D | ASP90 |
| D | ALA114 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:1906013, ECO:0000269|PubMed:8434007, ECO:0000269|PubMed:8706862 |
| Chain | Residue | Details |
| A | THR12 | |
| B | THR12 | |
| C | THR12 | |
| D | THR12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA |
| Chain | Residue | Details |
| A | SER58 | |
| A | THR89 | |
| B | SER58 | |
| B | THR89 | |
| C | SER58 | |
| C | THR89 | |
| D | SER58 | |
| D | THR89 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| A | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| A | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| A | LYS162 | proton acceptor, proton donor |
| A | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| A | GLU283 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| B | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| B | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| B | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| B | LYS162 | proton acceptor, proton donor |
| B | GLU283 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| C | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| C | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| C | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| C | LYS162 | proton acceptor, proton donor |
| C | GLU283 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| D | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| D | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| D | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| D | LYS162 | proton acceptor, proton donor |
| D | GLU283 | electrostatic stabiliser |
