3L7G
Crystal structure of organophosphate anhydrolase/prolidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004063 | molecular_function | aryldialkylphosphatase activity |
| 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 | 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 | 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 | 10 |
| Details | BINDING SITE FOR RESIDUE M44 A 518 |
| Chain | Residue |
| A | TYR212 |
| A | MN520 |
| A | ASP244 |
| A | ASP255 |
| A | HIS332 |
| A | HIS343 |
| A | GLU381 |
| A | ARG418 |
| A | GLU420 |
| A | MN519 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 519 |
| Chain | Residue |
| A | ASP255 |
| A | HIS336 |
| A | GLU381 |
| A | GLU420 |
| A | M44518 |
| A | MN520 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 520 |
| Chain | Residue |
| A | ASP244 |
| A | ASP255 |
| A | THR257 |
| A | GLU420 |
| A | M44518 |
| A | MN519 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 521 |
| Chain | Residue |
| A | HIS90 |
| A | HIS226 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN A 522 |
| Chain | Residue |
| A | ASP105 |
| A | GLU107 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE M44 B 518 |
| Chain | Residue |
| B | TYR212 |
| B | LEU225 |
| B | ASP244 |
| B | ASP255 |
| B | HIS332 |
| B | HIS343 |
| B | GLU381 |
| B | ARG418 |
| B | GLU420 |
| B | MN519 |
| B | MN520 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 519 |
| Chain | Residue |
| B | ASP255 |
| B | HIS336 |
| B | GLU381 |
| B | GLU420 |
| B | M44518 |
| B | MN520 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN B 520 |
| Chain | Residue |
| B | TYR212 |
| B | ASP244 |
| B | ASP255 |
| B | THR257 |
| B | GLU420 |
| B | M44518 |
| B | MN519 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 521 |
| Chain | Residue |
| B | GLU26 |
| C | GLU431 |
| C | GLU436 |
| C | HOH636 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN B 522 |
| Chain | Residue |
| B | HIS226 |
| C | HIS90 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE M44 C 518 |
| Chain | Residue |
| C | TYR212 |
| C | LEU225 |
| C | ASP244 |
| C | ASP255 |
| C | HIS343 |
| C | GLU381 |
| C | ARG418 |
| C | GLU420 |
| C | MN519 |
| C | MN520 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 519 |
| Chain | Residue |
| C | ASP255 |
| C | HIS336 |
| C | GLU381 |
| C | GLU420 |
| C | M44518 |
| C | MN520 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 520 |
| Chain | Residue |
| C | ASP244 |
| C | ASP255 |
| C | THR257 |
| C | GLU420 |
| C | M44518 |
| C | MN519 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MN C 521 |
| Chain | Residue |
| B | HIS90 |
| C | HIS226 |
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 | |
| B | GLU420 | |
| C | ASP244 | |
| C | ASP255 | |
| C | HIS336 | |
| C | GLU381 | |
| C | GLU420 | |
| A | ASP255 | |
| A | HIS336 | |
| A | GLU381 | |
| A | GLU420 | |
| B | ASP244 | |
| B | ASP255 | |
| B | HIS336 | |
| B | GLU381 |
