2DW6
Crystal structure of the mutant K184A of D-Tartrate Dehydratase from Bradyrhizobium japonicum complexed with Mg++ and D-tartrate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0034194 | biological_process | D-galactonate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0034194 | biological_process | D-galactonate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| B | 0051260 | biological_process | protein homooligomerization |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016836 | molecular_function | hydro-lyase activity |
| C | 0034194 | biological_process | D-galactonate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| C | 0051260 | biological_process | protein homooligomerization |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016836 | molecular_function | hydro-lyase activity |
| D | 0034194 | biological_process | D-galactonate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047808 | molecular_function | D(-)-tartrate dehydratase activity |
| D | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 2001 |
| Chain | Residue |
| A | ASP213 |
| A | GLU239 |
| A | GLU265 |
| A | TAR1001 |
| A | HOH2002 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | HOH2003 |
| B | ASP213 |
| B | GLU239 |
| B | GLU265 |
| B | TAR1002 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2003 |
| Chain | Residue |
| C | ASP213 |
| C | GLU239 |
| C | GLU265 |
| C | TAR1003 |
| C | HOH2004 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 2004 |
| Chain | Residue |
| D | LYS182 |
| D | ASP213 |
| D | GLU239 |
| D | GLU265 |
| D | TLA1004 |
| D | HOH2005 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TLA D 1004 |
| Chain | Residue |
| C | LYS102 |
| D | ASN21 |
| D | PHE26 |
| D | TYR156 |
| D | LYS182 |
| D | ASP213 |
| D | ASN215 |
| D | GLU239 |
| D | GLU265 |
| D | HIS322 |
| D | GLU341 |
| D | TYR343 |
| D | MG2004 |
| D | HOH2005 |
| D | HOH2112 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TAR A 1001 |
| Chain | Residue |
| A | ASN21 |
| A | PHE26 |
| A | ASN55 |
| A | TYR156 |
| A | LYS182 |
| A | ASP213 |
| A | ASN215 |
| A | GLU239 |
| A | GLU265 |
| A | HIS322 |
| A | GLU341 |
| A | TYR343 |
| A | MG2001 |
| A | HOH2002 |
| B | LYS102 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE TAR B 1002 |
| Chain | Residue |
| A | LYS102 |
| B | ASN21 |
| B | PHE26 |
| B | ASN55 |
| B | TYR156 |
| B | LYS182 |
| B | ASP213 |
| B | ASN215 |
| B | GLU239 |
| B | GLU265 |
| B | HIS322 |
| B | GLU341 |
| B | TYR343 |
| B | MG2002 |
| B | HOH2003 |
| B | HOH2073 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE TAR C 1003 |
| Chain | Residue |
| C | ASN21 |
| C | PHE26 |
| C | ASN55 |
| C | TYR156 |
| C | LYS182 |
| C | ASP213 |
| C | ASN215 |
| C | GLU239 |
| C | GLU265 |
| C | HIS322 |
| C | GLU341 |
| C | TYR343 |
| C | MG2003 |
| C | HOH2004 |
| C | HOH2040 |
| D | LYS102 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"acceptor","evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 56 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17144653","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Increases basicity of active site His"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| A | ASN55 | electrostatic stabiliser |
| A | LYS182 | electrostatic stabiliser |
| A | ALA184 | proton acceptor, proton donor |
| A | ASP213 | metal ligand |
| A | GLU239 | metal ligand |
| A | GLU265 | metal ligand |
| A | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| A | HIS322 | proton acceptor, proton donor |
| A | GLU341 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| B | ASN55 | electrostatic stabiliser |
| B | LYS182 | electrostatic stabiliser |
| B | ALA184 | proton acceptor, proton donor |
| B | ASP213 | metal ligand |
| B | GLU239 | metal ligand |
| B | GLU265 | metal ligand |
| B | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| B | HIS322 | proton acceptor, proton donor |
| B | GLU341 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| C | ASN55 | electrostatic stabiliser |
| C | LYS182 | electrostatic stabiliser |
| C | ALA184 | proton acceptor, proton donor |
| C | ASP213 | metal ligand |
| C | GLU239 | metal ligand |
| C | GLU265 | metal ligand |
| C | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| C | HIS322 | proton acceptor, proton donor |
| C | GLU341 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 463 |
| Chain | Residue | Details |
| D | ASN55 | electrostatic stabiliser |
| D | LYS182 | electrostatic stabiliser |
| D | ALA184 | proton acceptor, proton donor |
| D | ASP213 | metal ligand |
| D | GLU239 | metal ligand |
| D | GLU265 | metal ligand |
| D | ASP292 | electrostatic stabiliser, increase basicity, modifies pKa |
| D | HIS322 | proton acceptor, proton donor |
| D | GLU341 | electrostatic stabiliser |
