8ECE
E. coli L-asparaginase II mutant (V27T) in complex with L-Glu
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 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 | ASP90 | 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 | 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 |