4WDR
Crystal structure of haloalkane dehalogenase LinB 140A+143L+177W+211L mutant (LinB86) from Sphingobium japonicum UT26
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018786 | molecular_function | haloalkane dehalogenase activity |
| A | 0042597 | cellular_component | periplasmic space |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018786 | molecular_function | haloalkane dehalogenase activity |
| B | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | ASN38 |
| A | TRP109 |
| A | PRO208 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | ASP73 |
| A | ASP73 |
| A | ASP73 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 248 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10100638","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12939138","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14744129","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10100638","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12939138","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14744129","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10100638","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"12939138","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"14744129","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14744129","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14744129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17259360","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MJ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2BFN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 467 |
| Chain | Residue | Details |
| A | ASN38 | electrostatic stabiliser |
| A | ASP108 | covalent catalysis |
| A | TRP109 | electrostatic stabiliser |
| A | GLU132 | activator, electrostatic stabiliser |
| A | HIS272 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 467 |
| Chain | Residue | Details |
| B | ASN38 | electrostatic stabiliser |
| B | ASP108 | covalent catalysis |
| B | TRP109 | electrostatic stabiliser |
| B | GLU132 | activator, electrostatic stabiliser |
| B | HIS272 | activator, electrostatic stabiliser, proton shuttle (general acid/base) |
