3HLH
Diisopropyl fluorophosphatase (DFPase), active site mutants
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047862 | molecular_function | diisopropyl-fluorophosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 315 |
| Chain | Residue |
| A | GLU21 |
| A | ASN120 |
| A | ASN175 |
| A | ASP229 |
| A | HOH318 |
| A | HOH319 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 316 |
| Chain | Residue |
| A | HOH321 |
| A | HOH325 |
| A | HOH328 |
| A | ASP232 |
| A | LEU273 |
| A | HIS274 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 315 |
| Chain | Residue |
| A | PHE314 |
| B | GLU21 |
| B | ASN120 |
| B | ASN175 |
| B | ASP229 |
| B | HOH324 |
| B | HOH369 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 316 |
| Chain | Residue |
| B | ASP232 |
| B | LEU273 |
| B | HIS274 |
| B | HOH338 |
| B | HOH367 |
| B | HOH378 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA C 315 |
| Chain | Residue |
| B | PHE314 |
| C | GLU21 |
| C | ASN120 |
| C | ASN175 |
| C | ASP229 |
| C | HOH317 |
| C | HOH320 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 316 |
| Chain | Residue |
| C | ASP232 |
| C | LEU273 |
| C | HIS274 |
| C | HOH318 |
| C | HOH319 |
| C | HOH330 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 315 |
| Chain | Residue |
| D | GLU21 |
| D | ASN120 |
| D | ASN175 |
| D | ASP229 |
| D | HOH317 |
| D | HOH326 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 316 |
| Chain | Residue |
| D | ASP232 |
| D | LEU273 |
| D | HIS274 |
| D | HOH318 |
| D | HOH321 |
| D | HOH329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15966726 |
| Chain | Residue | Details |
| A | HIS287 | |
| B | HIS287 | |
| C | HIS287 | |
| D | HIS287 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLU21 | |
| C | ASN120 | |
| C | ASN175 | |
| C | ASP229 | |
| D | GLU21 | |
| D | ASN120 | |
| D | ASN175 | |
| D | ASP229 | |
| A | ASN120 | |
| A | ASN175 | |
| A | ASP229 | |
| B | GLU21 | |
| B | ASN120 | |
| B | ASN175 | |
| B | ASP229 | |
| C | GLU21 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 |
| Chain | Residue | Details |
| A | ASP232 | |
| D | ASP232 | |
| D | LEU273 | |
| D | HIS274 | |
| A | LEU273 | |
| A | HIS274 | |
| B | ASP232 | |
| B | LEU273 | |
| B | HIS274 | |
| C | ASP232 | |
| C | LEU273 | |
| C | HIS274 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1e1a |
| Chain | Residue | Details |
| A | HIS287 | |
| A | ALA37 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1e1a |
| Chain | Residue | Details |
| B | HIS287 | |
| B | ALA37 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1e1a |
| Chain | Residue | Details |
| C | HIS287 | |
| C | ALA37 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1e1a |
| Chain | Residue | Details |
| D | HIS287 | |
| D | ALA37 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 686 |
| Chain | Residue | Details |
| A | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
| A | ALA37 | electrostatic stabiliser, increase basicity |
| A | ASN120 | metal ligand |
| A | ASN175 | metal ligand |
| A | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
| A | HIS287 | increase nucleophilicity, proton acceptor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 686 |
| Chain | Residue | Details |
| B | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
| B | ALA37 | electrostatic stabiliser, increase basicity |
| B | ASN120 | metal ligand |
| B | ASN175 | metal ligand |
| B | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
| B | HIS287 | increase nucleophilicity, proton acceptor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 686 |
| Chain | Residue | Details |
| C | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
| C | ALA37 | electrostatic stabiliser, increase basicity |
| C | ASN120 | metal ligand |
| C | ASN175 | metal ligand |
| C | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
| C | HIS287 | increase nucleophilicity, proton acceptor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 686 |
| Chain | Residue | Details |
| D | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
| D | ALA37 | electrostatic stabiliser, increase basicity |
| D | ASN120 | metal ligand |
| D | ASN175 | metal ligand |
| D | ASP229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
| D | HIS287 | increase nucleophilicity, proton acceptor |
