MolNFT v1 · #25901 · protein
Crystal structure of 1,4-beta-D-xylan xylohydrolase solve using anomalous signal from seleniomethionine
1W91 · Beta-xylosidase: “Crystal structure of 1,4-beta-D-xylan xylohydrolase solve using anomalous signal from seleniomethionine”. X-ray diffraction, 20 pockets (best druggability 0.77). MolNFT v1 #25901 on GenesisL1: 3D structure, binding…
- PDB
- 1W91
- Type
- protein
- Length
- 3,992 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-xylosidase
- EC
- 3.1.2.37
- UniProt
- Q9ZFM2
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Beta-xylosidase (EC 3.1.2.37) | protein | 499 | 34% helix, 26% strand | Q9ZFM2 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 757 | 0.77 | 0.82 | 74 | empty |
| 2 | 679 | 0.77 | 0.82 | 81 | empty |
| 3 | 715 | 0.77 | 0.82 | 67 | empty |
| 4 | 776 | 0.77 | 0.81 | 69 | empty |
| 5 | 645 | 0.76 | 0.82 | 49 | empty |
Interfaces
14 interfaces between chains.
- E–G · 2730 Ų buried · 51 hydrogen bonds · protein-protein
- F–H · 2722 Ų buried · 54 hydrogen bonds · protein-protein
- A–C · 2709 Ų buried · 53 hydrogen bonds · protein-protein
- B–D · 2703 Ų buried · 49 hydrogen bonds · protein-protein
- E–H · 1696 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 1W91 · crystal structure of 1,4-BETA-D-XYLAN XYLOHYDROLASE solve using anomalous signal from… · the same entry in another collection · chain H against H, TM-score 1.00
- Q9ZFM2 · AlphaFold monomer V2.0 prediction for beta-xylosidase (Q9ZFM2) · a predicted model of the same protein · 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 Q9ZFM2
- Elsewhere: RCSB PDB 1W91 · PDBe 1W91 · UniProt Q9ZFM2
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