6V2A
Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asn
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 | L-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 | L-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 | L-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 | L-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 | 14 |
| Details | binding site for residue ASN A 401 |
| Chain | Residue |
| A | GLY11 |
| A | ASP90 |
| A | ALA114 |
| A | HOH533 |
| B | ASN248 |
| B | GLU283 |
| A | THR12 |
| A | TYR25 |
| A | VAL27 |
| A | GLY57 |
| A | SER58 |
| A | GLN59 |
| A | GLY88 |
| A | VAL89 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue ASN B 401 |
| Chain | Residue |
| A | ASN248 |
| A | GLU283 |
| B | GLY11 |
| B | THR12 |
| B | GLY57 |
| B | SER58 |
| B | GLN59 |
| B | GLY88 |
| B | VAL89 |
| B | ASP90 |
| B | ALA114 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ASN C 401 |
| Chain | Residue |
| C | GLY11 |
| C | THR12 |
| C | TYR25 |
| C | GLY57 |
| C | SER58 |
| C | GLN59 |
| C | GLY88 |
| C | VAL89 |
| C | ASP90 |
| C | ALA114 |
| C | HOH571 |
| D | ASN248 |
| D | GLU283 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue ASN D 401 |
| Chain | Residue |
| C | ASN248 |
| C | GLU283 |
| D | GLY11 |
| D | THR12 |
| D | VAL27 |
| D | GLY57 |
| D | SER58 |
| D | GLN59 |
| D | GLY88 |
| D | VAL89 |
| D | ASP90 |
| D | ALA114 |
| D | HOH619 |
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 | 972 |
| Details | Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"O-isoaspartyl threonine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12595697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1906013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8434007","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8706862","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12595697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8434007","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ECA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 | VAL89 | 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 | THR162 | proton acceptor, proton donor |
| A | GLU283 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 455 |
| Chain | Residue | Details |
| B | THR12 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | VAL89 | 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 | THR162 | 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 | VAL89 | 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 | THR162 | 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 | VAL89 | 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 | THR162 | proton acceptor, proton donor |
| D | GLU283 | electrostatic stabiliser |
