6WYX
Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase in complex with L-Asp at pH 5.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006528 | biological_process | asparagine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006528 | biological_process | asparagine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0050417 | molecular_function | glutamin-(asparagin-)ase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ASP A 400 |
| Chain | Residue |
| A | GLY19 |
| A | HOH546 |
| A | HOH618 |
| B | GLU294 |
| B | HOH520 |
| A | THR20 |
| A | ALA66 |
| A | SER67 |
| A | GLU68 |
| A | GLY99 |
| A | THR100 |
| A | ASP101 |
| A | SER125 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue ASP B 400 |
| Chain | Residue |
| A | GLU294 |
| A | HOH530 |
| B | GLY19 |
| B | THR20 |
| B | ALA66 |
| B | SER67 |
| B | GLU68 |
| B | GLY99 |
| B | THR100 |
| B | ASP101 |
| B | SER125 |
| B | HOH513 |
| B | HOH680 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | ALA83 |
| B | GLU87 |
| B | VAL113 |
| B | GLU114 |
| B | LYS115 |
| B | ASP214 |
| B | ILE215 |
| B | HOH562 |
| B | HOH575 |
| B | HOH692 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue ASP C 400 |
| Chain | Residue |
| C | GLY19 |
| C | THR20 |
| C | ALA66 |
| C | SER67 |
| C | GLU68 |
| C | GLY99 |
| C | THR100 |
| C | ASP101 |
| C | SER125 |
| C | HOH596 |
| C | HOH676 |
| C | HOH709 |
| D | GLU294 |
| D | HOH532 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue ASP D 400 |
| Chain | Residue |
| C | GLU294 |
| C | HOH531 |
| D | GLY19 |
| D | THR20 |
| D | ALA66 |
| D | SER67 |
| D | GLU68 |
| D | GLY99 |
| D | THR100 |
| D | ASP101 |
| D | SER125 |
| D | HOH518 |
| D | HOH520 |
| D | HOH667 |
| D | HOH728 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
