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 | 0008233 | molecular_function | peptidase activity |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | 0008233 | molecular_function | peptidase activity |
| B | 0008235 | molecular_function | metalloexopeptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016787 | molecular_function | hydrolase activity |
| 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 | 0008233 | molecular_function | peptidase activity |
| C | 0008235 | molecular_function | metalloexopeptidase activity |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0009636 | biological_process | response to toxic substance |
| C | 0016787 | molecular_function | hydrolase activity |
| 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 site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
