6V29
Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asp
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 | 10 |
| Details | binding site for residue ASP A 401 |
| Chain | Residue |
| A | GLY57 |
| B | GLU283 |
| A | SER58 |
| A | GLN59 |
| A | GLY88 |
| A | VAL89 |
| A | ASP90 |
| A | ALA114 |
| A | HOH637 |
| B | ASN248 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | LYS213 |
| A | TYR236 |
| B | SER224 |
| B | HOH613 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue ASP B 401 |
| Chain | Residue |
| A | ASN248 |
| A | GLU283 |
| B | GLY57 |
| B | SER58 |
| B | GLN59 |
| B | GLY88 |
| B | VAL89 |
| B | ASP90 |
| B | ALA114 |
| B | HOH590 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 402 |
| Chain | Residue |
| B | LYS172 |
| B | SER173 |
| B | VAL174 |
| B | ASN175 |
| B | TYR181 |
| B | HOH518 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue ASP C 401 |
| Chain | Residue |
| C | GLY57 |
| C | SER58 |
| C | GLN59 |
| C | GLY88 |
| C | VAL89 |
| C | ASP90 |
| C | ALA114 |
| C | HOH631 |
| D | ASN248 |
| D | GLU283 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | PRO193 |
| C | ALA194 |
| C | ARG195 |
| C | LYS196 |
| C | HIS197 |
| C | ASP200 |
| C | HOH504 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 403 |
| Chain | Residue |
| C | GLN280 |
| C | ASP286 |
| C | ALA287 |
| C | GLY290 |
| C | PHE291 |
| C | PRO316 |
| C | GLN317 |
| C | HOH569 |
| C | HOH585 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 404 |
| Chain | Residue |
| C | LYS172 |
| C | SER173 |
| C | VAL174 |
| C | ASN175 |
| C | TYR181 |
| C | HOH506 |
| C | HOH510 |
| C | HOH510 |
| C | HOH684 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | binding site for residue ASP D 401 |
| Chain | Residue |
| C | ASN248 |
| C | GLU283 |
| D | GLY57 |
| D | SER58 |
| D | GLN59 |
| D | GLY88 |
| D | VAL89 |
| D | ASP90 |
| D | ALA114 |
| D | HOH501 |
| D | HOH590 |
| D | HOH687 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 402 |
| Chain | Residue |
| D | GLN280 |
| D | ASP286 |
| D | GLY290 |
| D | PHE291 |
| D | PRO316 |
| D | GLN317 |
| D | GLN320 |
| D | HOH549 |
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 | 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 |
| B | THR12 | |
| C | THR12 | |
| D | THR12 | |
| A | 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 | VAL89 | |
| B | SER58 | |
| B | VAL89 | |
| C | SER58 | |
| C | VAL89 | |
| D | SER58 | |
| D | VAL89 |
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 | 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 | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| B | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| 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 | ASP90 | electrostatic stabiliser, increase acidity, increase basicity, increase nucleophilicity, proton acceptor, proton donor |
| C | VAL89 | electrostatic stabiliser, increase basicity, proton acceptor, proton donor, proton relay |
| 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 |
