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 | ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100 |
Chain | Residue | Details |
A | THR20 | |
B | THR20 | |
C | THR20 | |
D | THR20 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER67 | |
A | THR100 | |
B | SER67 | |
B | THR100 | |
C | SER67 | |
C | THR100 | |
D | SER67 | |
D | THR100 |