2YCE
Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.
Replaces: 1W8REntity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D, E... | FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1 | polymer | 263 | 28741.1 | 10 | UniProt (P58315) Pfam (PF01791) In PDB | THERMOPROTEUS TENAX | FRUCTOSE-BIPHOSPHATE ALDOLASE CLASS I, FBP ALDOLASE |
| 2 | A, B, C, D, E... | D-MANNITOL-1,6-DIPHOSPHATE | non-polymer | 342.1 | 10 | Chemie (M2P) | |||
| 3 | water | water | 18.0 | 1518 | Chemie (HOH) |
Sequence modifications
A, B, C, D, E, F, G, H, I, J: 1 - 263 (UniProt: P58315)
| PDB | External Database | Details |
|---|---|---|
| Phe 146 | Tyr 146 | engineered mutation |
| Ser 173 | Ala 173 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 10 |
| Total formula weight | 287410.6 | |
| Non-Polymers* | Number of molecules | 10 |
| Total formula weight | 3421.3 | |
| All* | Total formula weight | 290832.0 |
