3L24
Crystal Structure of the Nerve Agent Degrading Organophosphate Anhydrolase/Prolidase in Complex with Inhibitors
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004063 | molecular_function | aryldialkylphosphatase activity |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0008235 | molecular_function | metalloexopeptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0009636 | biological_process | response to toxic substance |
A | 0016795 | molecular_function | phosphoric triester hydrolase activity |
A | 0016805 | molecular_function | dipeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
A | 0102009 | molecular_function | proline dipeptidase activity |
B | 0004063 | molecular_function | aryldialkylphosphatase activity |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0008235 | molecular_function | metalloexopeptidase activity |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0009636 | biological_process | response to toxic substance |
B | 0016795 | molecular_function | phosphoric triester hydrolase activity |
B | 0016805 | molecular_function | dipeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
B | 0102009 | molecular_function | proline dipeptidase activity |
C | 0004063 | molecular_function | aryldialkylphosphatase activity |
C | 0004177 | molecular_function | aminopeptidase activity |
C | 0005829 | cellular_component | cytosol |
C | 0006508 | biological_process | proteolysis |
C | 0008235 | molecular_function | metalloexopeptidase activity |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0009636 | biological_process | response to toxic substance |
C | 0016795 | molecular_function | phosphoric triester hydrolase activity |
C | 0016805 | molecular_function | dipeptidase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
C | 0102009 | molecular_function | proline dipeptidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 518 |
Chain | Residue |
A | ASP255 |
A | HIS336 |
A | GLU381 |
A | GLU420 |
A | MN519 |
A | GOA521 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 519 |
Chain | Residue |
A | GLU420 |
A | MN518 |
A | GOA521 |
A | ASP244 |
A | ASP255 |
A | THR257 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 520 |
Chain | Residue |
A | ASP105 |
A | GLU107 |
A | HOH648 |
A | HOH674 |
A | HOH675 |
A | HOH676 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOA A 521 |
Chain | Residue |
A | TYR212 |
A | ASP244 |
A | ASP255 |
A | HIS343 |
A | GLU381 |
A | GLU420 |
A | MN518 |
A | MN519 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 518 |
Chain | Residue |
B | ASP255 |
B | HIS336 |
B | GLU381 |
B | GLU420 |
B | MN519 |
B | GOA522 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 519 |
Chain | Residue |
B | ASP244 |
B | ASP255 |
B | THR257 |
B | GLU420 |
B | MN518 |
B | GOA522 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 520 |
Chain | Residue |
B | GLU26 |
B | HOH602 |
B | HOH627 |
C | GLU436 |
C | HOH603 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN B 521 |
Chain | Residue |
B | HIS226 |
C | HIS90 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOA B 522 |
Chain | Residue |
B | TYR212 |
B | ASP244 |
B | ASP255 |
B | HIS336 |
B | HIS343 |
B | GLU381 |
B | GLU420 |
B | MN518 |
B | MN519 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 518 |
Chain | Residue |
C | ASP255 |
C | HIS336 |
C | GLU381 |
C | GLU420 |
C | MN519 |
C | GOA521 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN C 519 |
Chain | Residue |
C | ASP244 |
C | ASP255 |
C | THR257 |
C | GLU420 |
C | MN518 |
C | GOA521 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MN C 520 |
Chain | Residue |
B | HIS90 |
C | HIS226 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOA C 521 |
Chain | Residue |
C | TYR212 |
C | ASP244 |
C | ASP255 |
C | HIS336 |
C | HIS343 |
C | GLU381 |
C | GLU420 |
C | MN518 |
C | MN519 |
Functional Information from PROSITE/UniProt
site_id | PS00491 |
Number of Residues | 13 |
Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHhIGLqVHD |
Chain | Residue | Details |
A | HIS332-ASP344 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 15 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP244 | |
A | ASP255 | |
B | GLU420 | |
C | ASP244 | |
C | ASP255 | |
C | HIS336 | |
C | GLU381 | |
C | GLU420 | |
A | HIS336 | |
A | GLU381 | |
A | GLU420 | |
B | ASP244 | |
B | ASP255 | |
B | HIS336 | |
B | GLU381 |