1M75
Crystal Structure of the N208S Mutant of L-3-Hydroxyacyl-COA Dehydrogenase in Complex with NAD and Acetoacetyl-COA
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) | 3-HYDROXYACYL-COA DEHYDROGENASE | polymer | 302 | 32841.7 | 2 | UniProt (Q16836) Pfam (PF02737) Pfam (PF00725) | Homo sapiens (human) | L-3-HYDROXYACYL-COA DEHYDROGENASE |
| 2 | C, E (A, B) | ACETOACETYL-COENZYME A | non-polymer | 851.6 | 2 | Chemie (CAA) | |||
| 3 | D, F (A, B) | NICOTINAMIDE-ADENINE-DINUCLEOTIDE | non-polymer | 663.4 | 2 | Chemie (NAD) | |||
| 4 | G, H (A, B) | water | water | 18.0 | 223 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 302 (UniProt: Q16836)
| PDB | External Database | Details |
|---|---|---|
| Ser 208 | Asn 220 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 65683.4 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 3030.1 | |
| All* | Total formula weight | 68713.4 |
