Research workbench
Respective role of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase a
Analyse Respective role of protein folding and glycosylation in the thermal stability… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IX9
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Feruloyl esterase a
- EC
- 3.1.1.73
- UniProt
- O42807
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Feruloyl esterase a (EC 3.1.1.73) | protein | 260 | 34% helix, 25% strand | O42807 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 495 | 0.76 | 0.84 | 69 | CXS, EDO |
| 2 | 95 | 0.46 | 0.80 | 24 | SO4 |
| 3 | 97 | 0.45 | 0.80 | 24 | SO4 |
Interfaces
1 interface between chains.
- A–B · 643 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2IX9 · Respective role of protein folding and glycosylation in the thermal stability of… · the same entry in another collection · chain A against A, TM-score 1.00
- O42807 · AlphaFold monomer V2.0 prediction for feruloyl esterase a (O42807) · a predicted model of the same protein · chain B against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O42807
- Elsewhere: RCSB PDB 2IX9 · PDBe 2IX9 · UniProt O42807
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