1UXG
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 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 activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| 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 | GLN143 |
| A | LEU147 |
| A | HIS175 |
| A | PHE12 |
| A | PRO229 |
| A | FUM1311 |
| A | HOH2142 |
| A | HOH2199 |
| A | HOH2200 |
| A | HOH2201 |
| A | HOH2202 |
| A | HOH2203 |
| A | HOH2204 |
| A | HOH2205 |
| A | VAL13 |
| A | HOH2206 |
| A | ASP33 |
| A | ILE34 |
| A | VAL35 |
| A | TYR65 |
| A | THR77 |
| A | SER78 |
| site_id | AC2 |
| Number of Residues | 10 |
| 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 | HOH2206 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 1310 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | PHE12 |
| B | VAL13 |
| 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 | GLN143 |
| B | LEU147 |
| B | HIS175 |
| B | PRO229 |
| B | FUM1311 |
| B | HOH2009 |
| B | HOH2048 |
| B | HOH2141 |
| B | HOH2198 |
| B | HOH2199 |
| B | HOH2201 |
| B | HOH2202 |
| B | HOH2203 |
| B | HOH2204 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FUM B 1311 |
| Chain | Residue |
| B | ARG82 |
| B | ARG88 |
| B | LEU147 |
| B | ARG151 |
| B | HIS175 |
| B | GLY213 |
| B | SER224 |
| B | NAD1310 |
| B | HOH2129 |
| B | HOH2204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-Rule:MF_00487 |
| Chain | Residue | Details |
| A | HIS175 | |
| B | HIS175 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000269|PubMed:12054817, ECO:0000269|PubMed:14636605 |
| Chain | Residue | Details |
| A | VAL118 | |
| B | GLY9 | |
| B | ASP33 | |
| B | VAL118 | |
| A | GLY9 | |
| A | ASP33 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889, ECO:0000255|HAMAP-Rule:MF_00487 |
| Chain | Residue | Details |
| A | ASN95 | |
| A | ASN120 | |
| A | ARG151 | |
| B | ARG82 | |
| B | ARG88 | |
| B | ASN95 | |
| B | ASN120 | |
| B | ARG151 | |
| A | ARG82 | |
| A | ARG88 |
