MolNFT v1 · #59748 · protein
Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus subtilis.
3C7E · Endo-1,4-beta-xylanase: “Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase from bacillus…”. X-ray diffraction, 2 ligands (NA, CA), 4 pockets (best druggability 0.64). MolNFT v1 #59748 on…
- PDB
- 3C7E
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-1,4-beta-xylanase
- EC
- 3.2.1.55
- UniProt
- Q45071
- Ligands
- NA, CA
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-1,4-beta-xylanase (EC 3.2.1.55) | protein | 487 | 3% helix, 43% strand | Q45071 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A
- CA · Calcium ion · metal · chains A
- FMT · Formic acid · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.64 | 0.81 | 33 | NA |
| 2 | 105 | 0.47 | 0.80 | 21 | FMT |
| 3 | 131 | 0.39 | 0.74 | 23 | empty |
| 4 | 105 | 0.37 | 0.75 | 17 | empty |
Compared structures
- 3C7E · Crystal structure of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q45071 · AlphaFold monomer V2.0 prediction for arabinoxylan arabinofuranohydrolase (Q45071) · 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 Q45071
- Elsewhere: RCSB PDB 3C7E · PDBe 3C7E · UniProt Q45071
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