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 | 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 |