1BMD
DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | MALATE DEHYDROGENASE | polymer | 327 | 35452.7 | 2 | UniProt (P10584) | Thermus thermophilus | |
| 2 | C, D (A, B) | NICOTINAMIDE-ADENINE-DINUCLEOTIDE | non-polymer | 663.4 | 2 | Chemie (NAD) | |||
| 3 | E, F (A, B) | water | water | 18.0 | 288 | Chemie (HOH) |
Sequence modifications
A, B: 0 - 332 (UniProt: P10584)
| PDB | External Database | Details |
|---|---|---|
| Asp 74 | Lys 75 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 70905.4 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 1326.8 | |
| All* | Total formula weight | 72232.2 |
