1UXH
Large improvement in the thermal stability of a tetrameric malate dehydrogenase by single point mutations at the dimer-dimer interface
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 1310 |
| Chain | Residue |
| A | GLY11 |
| A | GLY79 |
| A | ALA80 |
| A | PRO81 |
| A | ASN95 |
| A | CYS102 |
| A | VAL118 |
| A | ASN120 |
| A | LEU122 |
| A | GLN143 |
| A | LEU147 |
| A | PHE12 |
| A | HIS175 |
| A | PRO229 |
| A | FUM1311 |
| A | HOH2233 |
| A | HOH2234 |
| A | HOH2235 |
| A | HOH2236 |
| A | HOH2237 |
| A | HOH2238 |
| A | HOH2239 |
| A | VAL13 |
| A | HOH2240 |
| A | HOH2241 |
| A | ASP33 |
| A | ILE34 |
| A | VAL35 |
| A | TYR65 |
| A | THR77 |
| A | SER78 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE FUM A 1311 |
| Chain | Residue |
| A | ARG82 |
| A | ARG88 |
| A | ASN120 |
| A | LEU147 |
| A | ARG151 |
| A | HIS175 |
| A | GLY213 |
| A | SER224 |
| A | NAD1310 |
| A | HOH2154 |
| A | HOH2240 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 1310 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | PHE12 |
| B | VAL13 |
| B | LEU32 |
| B | ASP33 |
| B | ILE34 |
| B | VAL35 |
| B | TYR65 |
| B | THR77 |
| B | SER78 |
| B | GLY79 |
| B | ALA80 |
| B | PRO81 |
| B | ASN95 |
| B | CYS102 |
| B | VAL118 |
| B | ASN120 |
| B | LEU122 |
| B | GLN143 |
| B | LEU147 |
| B | HIS175 |
| B | PRO229 |
| B | FUM1311 |
| B | HOH2011 |
| B | HOH2154 |
| B | HOH2205 |
| B | HOH2206 |
| B | HOH2207 |
| B | HOH2208 |
| B | HOH2209 |
| B | HOH2211 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FUM B 1311 |
| Chain | Residue |
| B | ARG82 |
| B | ARG88 |
| B | ASN120 |
| B | LEU147 |
| B | ARG151 |
| B | HIS175 |
| B | GLY213 |
| B | SER224 |
| B | NAD1310 |
| B | HOH2211 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12054817","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14636605","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00487","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS175 | |
| A | ASP148 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS175 | |
| B | ASP148 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| A | HIS175 | |
| A | ASP148 | |
| A | ARG151 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1emd |
| Chain | Residue | Details |
| B | HIS175 | |
| B | ASP148 | |
| B | ARG151 |
