3KGG
X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 500 |
Chain | Residue |
A | GLU21 |
A | ASN120 |
A | ASN175 |
A | ASP229 |
A | HOH322 |
A | HOH323 |
A | HOH324 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 501 |
Chain | Residue |
A | HIS274 |
A | HOH326 |
A | HOH327 |
A | HOH331 |
A | ASP232 |
A | LEU273 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15966726 |
Chain | Residue | Details |
A | HIS287 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | GLU21 | |
A | ASN120 | |
A | ASN175 | |
A | ASP229 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11435114, ECO:0000269|PubMed:14501113 |
Chain | Residue | Details |
A | ASP232 | |
A | LEU273 | |
A | HIS274 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 686 |
Chain | Residue | Details |
A | GLU21 | increase nucleophilicity, metal ligand, proton acceptor |
A | GLU37 | 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 |