2IX9
Respective role of protein folding and glycosylation in the thermal stability of recombinant Feruloyl Esterase A
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B | FERULOYL ESTERASE A | polymer | 260 | 28372.9 | 2 | UniProt (O42807) Pfam (PF01764) In PDB | ASPERGILLUS NIGER | FERULOYL ESTERASE TYPE A, FAE-III, CINNAMOYL ESTERASE |
| 2 | A, B | 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID | non-polymer | 221.3 | 2 | Chemie (CXS) | |||
| 3 | A, B | 1,2-ETHANEDIOL | non-polymer | 62.1 | 8 | Chemie (EDO) | |||
| 4 | A, B | SULFATE ION | non-polymer | 96.1 | 2 | Chemie (SO4) | |||
| 5 | water | water | 18.0 | 525 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 260 (UniProt: O42807)
| PDB | External Database | Details |
|---|---|---|
| Glu 203 | Asp 224 | conflict |
| Gln 204 | Glu 225 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 56745.8 | |
| Non-Polymers* | Number of molecules | 12 |
| Total formula weight | 1131.3 | |
| All* | Total formula weight | 57877.1 |
