6WYY
Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase in complex with L-Glu at pH 6.5
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 GLU A 400 |
| Chain | Residue |
| A | GLY19 |
| A | HOH502 |
| A | HOH581 |
| A | HOH695 |
| B | GLU294 |
| A | THR20 |
| A | ALA66 |
| A | SER67 |
| A | GLU68 |
| A | GLY99 |
| A | THR100 |
| A | ASP101 |
| A | SER125 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | ALA16 |
| A | THR17 |
| A | GLY18 |
| A | ALA22 |
| A | GLY40 |
| A | GLN61 |
| A | GLN64 |
| A | THR97 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | LYS205 |
| A | TRP335 |
| A | HOH506 |
| A | HOH595 |
| A | HOH716 |
| D | TRP199 |
| D | HOH641 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue GLU B 400 |
| Chain | Residue |
| A | GLU294 |
| B | GLY19 |
| B | THR20 |
| B | ALA66 |
| B | SER67 |
| B | GLU68 |
| B | GLY99 |
| B | THR100 |
| B | ASP101 |
| B | SER125 |
| B | HOH505 |
| B | HOH549 |
| B | HOH648 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 401 |
| Chain | Residue |
| B | ARG81 |
| B | GLU84 |
| B | HOH720 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ASN292 |
| B | ALA293 |
| B | GLU294 |
| B | GLN295 |
| B | PRO296 |
| B | HOH615 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue GLU C 400 |
| Chain | Residue |
| C | GLY19 |
| C | THR20 |
| C | ALA66 |
| C | SER67 |
| C | GLU68 |
| C | GLY99 |
| C | THR100 |
| C | ASP101 |
| C | SER125 |
| C | HOH608 |
| C | HOH645 |
| D | GLU294 |
| D | HOH516 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | ALA32 |
| C | THR33 |
| C | TYR34 |
| C | HOH550 |
| C | HOH725 |
| D | ALA293 |
| D | GLU294 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 402 |
| Chain | Residue |
| C | ASP92 |
| C | ALA147 |
| C | SER148 |
| C | ASP149 |
| C | ARG153 |
| C | HOH504 |
| C | HOH614 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue GLU D 400 |
| Chain | Residue |
| C | GLU294 |
| D | GLY19 |
| D | THR20 |
| D | ALA66 |
| D | SER67 |
| D | GLU68 |
| D | GLY99 |
| D | THR100 |
| D | ASP101 |
| D | SER125 |
| D | HOH555 |
| D | HOH659 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 401 |
| Chain | Residue |
| B | LYS272 |
| D | PRO222 |
| D | LYS247 |
| D | MET321 |
| D | GLN325 |
| D | HOH503 |
| D | HOH660 |
| D | HOH740 |
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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 654 |
| Details | Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






