1JJA
CRYSTAL STRUCTURE OF ORTHORHOMBIC FORM OF D90E MUTANT OF ESCHERICHIA COLI L-ASPARAGINASE II
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 |
| E | 0004067 | molecular_function | asparaginase activity |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006528 | biological_process | asparagine metabolic process |
| E | 0006530 | biological_process | asparagine catabolic process |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0051289 | biological_process | protein homotetramerization |
| F | 0004067 | molecular_function | asparaginase activity |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006528 | biological_process | asparagine metabolic process |
| F | 0006530 | biological_process | asparagine catabolic process |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| F | 0032991 | cellular_component | protein-containing complex |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0051289 | biological_process | protein homotetramerization |
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 | ILE6-ALA14 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | |
| E | THR12 | |
| F | THR12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12595697, ECO:0000269|PubMed:8434007, ECO:0007744|PDB:1NNS, ECO:0007744|PDB:3ECA |
| Chain | Residue | Details |
| A | SER58 | |
| E | THR89 | |
| F | SER58 | |
| F | THR89 | |
| A | THR89 | |
| B | SER58 | |
| B | THR89 | |
| C | SER58 | |
| C | THR89 | |
| D | SER58 | |
| D | THR89 | |
| E | SER58 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | GLU90 | |
| A | THR12 | |
| A | LYS162 | |
| A | THR89 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | THR12 | |
| A | THR89 | |
| C | GLU283 |
| site_id | CSA11 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | GLU283 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| F | THR89 | |
| F | THR12 | |
| E | GLU283 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| F | GLU283 | |
| E | THR12 | |
| E | THR89 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| B | GLU90 | |
| B | THR12 | |
| B | LYS162 | |
| B | THR89 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| C | GLU90 | |
| C | TYR25 | |
| C | THR89 | |
| C | THR12 | |
| C | LYS162 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | GLU90 | |
| D | THR12 | |
| D | LYS162 | |
| D | THR89 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| E | GLU90 | |
| E | THR12 | |
| E | LYS162 | |
| E | THR89 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| F | GLU90 | |
| F | THR12 | |
| F | LYS162 | |
| F | THR89 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| B | THR12 | |
| B | THR89 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | GLU283 | |
| C | TYR25 | |
| C | THR89 | |
| C | THR12 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | THR89 | |
| D | THR12 | |
| B | GLU283 |
| 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 | GLU90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| A | LYS162 | 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 | GLU90 | 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 | GLU90 | 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 | GLU90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| D | LYS162 | proton acceptor, proton donor |
| D | GLU283 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| E | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| E | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| E | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| E | GLU90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| E | LYS162 | proton acceptor, proton donor |
| E | GLU283 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 6 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| F | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| F | TYR25 | electrostatic stabiliser, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| F | THR89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| F | GLU90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| F | LYS162 | proton acceptor, proton donor |
| F | GLU283 | electrostatic stabiliser |
