1OLU
Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | 2-OXOISOVALERATE DEHYDROGENASE ALPHA SUBUNIT | polymer | 400 | 45504.0 | 1 | UniProt (P12694) Pfam (PF00676) In PDB | HOMO SAPIENS (HUMAN) | BRANCHED-CHAIN ALPHA-KETOACID DEHYDROGENASE E1 COMPONENT ALPHA CHAIN, BCKDH E1-ALPHA |
| 2 | B | 2-OXOISOVALERATE DEHYDROGENASE BETA SUBUNIT | polymer | 342 | 37902.3 | 1 | UniProt (P21953) Pfam (PF02779) Pfam (PF02780) In PDB | HOMO SAPIENS (HUMAN) | BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE E1 COMPONENT BETA CHAIN, BCKDH E1-BETA |
| 3 | A, B | POTASSIUM ION | non-polymer | 39.1 | 2 | Chemie (K) | |||
| 4 | A | MAGNESIUM ION | non-polymer | 24.3 | 1 | Chemie (MG) | |||
| 5 | A | THIAMINE DIPHOSPHATE | non-polymer | 425.3 | 1 | Chemie (TPP) | |||
| 6 | A, B | GLYCEROL | non-polymer | 92.1 | 4 | Chemie (GOL) | |||
| 7 | water | water | 18.0 | 540 | Chemie (HOH) |
Sequence modifications
A: 1 - 400 (UniProt: P12694)
| PDB | External Database | Details |
|---|---|---|
| Ala 291 | His 336 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 83406.3 | |
| Non-Polymers* | Number of molecules | 8 |
| Total formula weight | 896.2 | |
| All* | Total formula weight | 84302.5 |
