Research workbench
Enzyme-substrate interactions of IXT6, the intracellular xylanase of G. stearothermophilus.
Analyse Enzyme-substrate interactions of IXT6, the intracellular xylanase of G.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MS8
- Type
- protein
- Length
- 658 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intra-cellular xylanase IXT6
- EC
- 3.2.1.8
- UniProt
- Q09LY9
- Ligands
- NA
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Intra-cellular xylanase IXT6 (EC 3.2.1.8) | protein | 330 | 40% helix, 19% strand | Q09LY9 |
| B | Intra-cellular xylanase IXT6 (EC 3.2.1.8) | protein | 328 | 40% helix, 18% strand | Q09LY9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.67 | 0.82 | 47 | GOL |
| 2 | 305 | 0.64 | 0.80 | 38 | GOL |
| 3 | 290 | 0.54 | 0.75 | 30 | GOL |
| 4 | 51 | 0.26 | 0.74 | 11 | GOL |
Interfaces
1 interface between chains.
- A–B · 584 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3MS8 · Enzyme-Substrate interactions of IXT6, the intracellular xylanase of G.… · the same entry in another collection · chain A 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 Q09LY9
- Elsewhere: RCSB PDB 3MS8 · PDBe 3MS8 · UniProt Q09LY9
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