MolNFT v1 · #40592 · protein
Respective role of protein folding and glycosylation in the thermal stability of recombinant feruloyl esterase a
2IX9: “Respective role of protein folding and glycosylation in the thermal stability of recombinant feruloyl…”. X-ray diffraction. MolNFT v1 #40592 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IX9
- Type
- protein
- Length
- 520 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O42807
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 260 | — | O42807 |
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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