Research workbench
Structural basis for the substrate specificity of the ferul domain of the cellulosomal xylanase Z from C. thermocellum
Analyse Structural basis for the substrate specificity of the ferul domain of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JT2
- Type
- protein
- Length
- 255 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (endo-1,4-beta-xylanase Z)
- EC
- 3.2.1.8
- UniProt
- P10478
- Ligands
- FER
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (endo-1,4-beta-xylanase Z) (EC 3.2.1.8) | protein | 255 | 33% helix, 21% strand | P10478 |
Ligands and binding sites
- FER · 3-(4-hydroxy-3-methoxyphenyl)-2-propenoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1JT2 · Structural basis for the substrate specificity of the ferul domain of the cellulosomal… · the same entry in another collection · chain A against A, TM-score 1.00
- P10478 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Z (P10478) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P10478
- Elsewhere: RCSB PDB 1JT2 · PDBe 1JT2 · UniProt P10478
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.