5I3Z
Erwinia chrysanthemi L-asparaginase E63Q mutation + Aspartic acid
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 | 0016787 | molecular_function | hydrolase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006528 | biological_process | asparagine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006528 | biological_process | asparagine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue ASP A 400 |
| Chain | Residue |
| A | GLY14 |
| A | HOH515 |
| A | HOH592 |
| A | THR15 |
| A | ALA61 |
| A | SER62 |
| A | GLN63 |
| A | GLY94 |
| A | THR95 |
| A | ASP96 |
| A | ALA120 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ASP B 400 |
| Chain | Residue |
| B | GLY14 |
| B | THR15 |
| B | ALA61 |
| B | SER62 |
| B | GLN63 |
| B | GLY94 |
| B | THR95 |
| B | ASP96 |
| B | ALA120 |
| B | HOH548 |
| B | HOH556 |
| B | HOH625 |
| B | HOH642 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ASP C 400 |
| Chain | Residue |
| C | GLY14 |
| C | THR15 |
| C | ALA61 |
| C | SER62 |
| C | GLN63 |
| C | GLY94 |
| C | THR95 |
| C | ASP96 |
| C | ALA120 |
| C | HOH521 |
| C | HOH553 |
| C | HOH599 |
| C | HOH693 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue ASP D 400 |
| Chain | Residue |
| D | GLY14 |
| D | THR15 |
| D | ALA61 |
| D | SER62 |
| D | GLN63 |
| D | GLY94 |
| D | THR95 |
| D | ASP96 |
| D | ALA120 |
| D | HOH507 |
| D | HOH579 |
| D | HOH589 |
| D | HOH658 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1288 |
| 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":"11755201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8348975","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
