Research workbench
Crystal structure of xeg-xyloglucan
Analyse Crystal structure of xeg-xyloglucan in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VL9
- Type
- protein
- Length
- 443 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xyloglucan-specific endo-beta-1,4-glucanase a
- EC
- 3.2.1.151
- UniProt
- O94218
- Ligands
- BGC, XYS
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xyloglucan-specific endo-beta-1,4-glucanase a (EC 3.2.1.151) | protein | 222 | 7% helix, 57% strand | O94218 |
| B | Xyloglucan-specific endo-beta-1,4-glucanase a (EC 3.2.1.151) | protein | 221 | 7% helix, 57% strand | O94218 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 8 copies · chains A, B
- XYS · alpha-D-xylopyranose · sugar · 3 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 | 614 | 0.64 | 0.75 | 62 | BGC, XYS |
| 2 | 124 | 0.40 | 0.75 | 28 | BGC |
Interfaces
1 interface between chains.
- A–B · 271 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 O94218
- Elsewhere: RCSB PDB 3VL9 · PDBe 3VL9 · UniProt O94218
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