1UXK
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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0030060 | molecular_function | L-malate dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 1308 |
Chain | Residue |
A | ASP200 |
A | ASP243 |
A | GLU277 |
A | HOH2280 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 1309 |
Chain | Residue |
A | GLU195 |
A | GLU281 |
A | HOH2206 |
C | GLU281 |
C | CL1312 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 1310 |
Chain | Residue |
A | GLU159 |
A | HOH2168 |
A | HOH2170 |
C | GLU159 |
C | HOH2219 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 1311 |
Chain | Residue |
A | GLU178 |
A | CL1313 |
A | HOH2077 |
A | HOH2142 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 1312 |
Chain | Residue |
A | ASP148 |
A | HIS175 |
A | HOH2162 |
A | HOH2185 |
A | HOH2314 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1313 |
Chain | Residue |
A | ASP123 |
A | ALA124 |
A | THR302 |
A | CD1311 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1314 |
Chain | Residue |
A | HIS19 |
A | HIS19 |
A | HOH2008 |
A | HOH2008 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 1315 |
Chain | Residue |
A | TYR226 |
A | HOH2007 |
A | HOH2007 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1316 |
Chain | Residue |
A | ARG2 |
A | LYS3 |
A | LEU26 |
C | HOH2258 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD A 1317 |
Chain | Residue |
A | HOH2052 |
A | HOH2054 |
A | HOH2247 |
A | HOH2250 |
A | HOH2251 |
C | HOH2176 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 1318 |
Chain | Residue |
A | HOH2078 |
A | HOH2079 |
A | HOH2184 |
A | HOH2188 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 1319 |
Chain | Residue |
C | TYR226 |
C | TYR226 |
C | HOH2250 |
C | HOH2250 |
C | HOH2251 |
C | HOH2251 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD C 1310 |
Chain | Residue |
C | ASP148 |
C | HIS175 |
C | HOH2153 |
C | HOH2156 |
C | HOH2159 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD C 1311 |
Chain | Residue |
C | GLU178 |
C | HOH2136 |
C | HOH2139 |
C | HOH2190 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 1312 |
Chain | Residue |
A | GLU281 |
A | CD1309 |
A | HOH2204 |
C | GLU281 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD C 1313 |
Chain | Residue |
A | HOH2178 |
C | HOH2047 |
C | HOH2048 |
C | HOH2050 |
C | HOH2253 |
C | HOH2254 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD C 1314 |
Chain | Residue |
C | HOH2129 |
C | HOH2204 |
C | HOH2207 |
C | HOH2270 |
C | HOH2289 |
C | HOH2290 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA C 1315 |
Chain | Residue |
A | ASP243 |
site_id | CC1 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD A 1307 |
Chain | Residue |
A | HIS175 |
A | PRO229 |
A | HOH2075 |
A | HOH2244 |
A | HOH2312 |
A | HOH2313 |
A | HOH2314 |
A | HOH2315 |
A | HOH2316 |
A | HOH2317 |
A | HOH2318 |
A | HOH2319 |
A | HOH2320 |
A | GLY9 |
A | GLY11 |
A | PHE12 |
A | VAL13 |
A | ASP33 |
A | ILE34 |
A | VAL35 |
A | TYR65 |
A | THR77 |
A | SER78 |
A | GLY79 |
A | ALA80 |
A | ILE98 |
A | CYS102 |
A | VAL118 |
A | ASN119 |
A | ASN120 |
A | GLN143 |
A | LEU147 |
site_id | CC2 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD C 1309 |
Chain | Residue |
C | GLY9 |
C | GLY11 |
C | PHE12 |
C | VAL13 |
C | ASP33 |
C | ILE34 |
C | VAL35 |
C | TYR65 |
C | THR77 |
C | SER78 |
C | GLY79 |
C | ALA80 |
C | ILE98 |
C | CYS102 |
C | VAL118 |
C | ASN120 |
C | GLN143 |
C | LEU147 |
C | HIS175 |
C | PRO229 |
C | HOH2069 |
C | HOH2153 |
C | HOH2246 |
C | HOH2247 |
C | HOH2319 |
C | HOH2320 |
C | HOH2321 |
C | HOH2322 |
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 | |
C | 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 | |
C | GLY9 | |
C | ASP33 | |
C | 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 | |
C | ARG82 | |
C | ARG88 | |
C | ASN95 | |
C | ASN120 | |
C | ARG151 | |
A | ARG82 | |
A | ARG88 |