MolNFT v2 · #213102 · protein
Crystal structure of GH11 from Thermoanaerobacterium saccharolyticum
8IH0 · Endo-1,4-beta-xylanase: “Crystal structure of GH11 from Thermoanaerobacterium saccharolyticum”. X-ray diffraction at 1.5, 2 pockets (best druggability 0.55). MolNFT v2 #213102 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 8IH0
- Type
- protein
- Length
- 367 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Thermoanaerobacterium saccharolyticum
- Molecule
- Endo-1,4-beta-xylanase
- UniProt
- I3VTR8
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · resolution 1.5 · 2 distinct chains · 5% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase | protein | 184 | 5% helix, 64% strand | I3VTR8 |
| B | Endo-1,4-beta-xylanase | protein | 183 | 5% helix, 64% strand | I3VTR8 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.55 | 0.75 | 46 | empty |
| 2 | 155 | 0.46 | 0.76 | 27 | ACT |
Interfaces
1 interface between chains.
- A–B · 383 Ų buried · 5 hydrogen bonds · protein-protein
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 I3VTR8
- Elsewhere: RCSB PDB 8IH0 · PDBe 8IH0 · UniProt I3VTR8
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