3LI4
Diisopropyl fluorophosphatase (DFPase), N120D,N175D,D229N mutant
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 315 |
| Chain | Residue |
| A | ASP232 |
| A | LEU273 |
| A | HIS274 |
| A | HOH320 |
| A | HOH321 |
| A | HOH323 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 316 |
| Chain | Residue |
| A | ASN229 |
| A | HOH324 |
| A | HOH327 |
| A | HOH330 |
| A | GLU21 |
| A | ASP120 |
| A | ASP175 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15966726","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11435114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14501113","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | ASP120 | metal ligand |
| A | ASP175 | metal ligand |
| A | ASN229 | covalently attached, electrofuge, electrophile, increase nucleophilicity, metal ligand, nucleophile, proton acceptor |
| A | HIS287 | increase nucleophilicity, proton acceptor |
