Research workbench
High-resolution structure of XACCEL5A in complex with cellopentaose
Analyse High-resolution structure of XACCEL5A in complex with cellopentaose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4W7W
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulase
- UniProt
- Q8PRD3
- Ligands
- BGC, GLC
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulase | protein | 313 | 35% helix, 18% strand | Q8PRD3 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.40 | 0.75 | 26 | BGC |
| 2 | 53 | 0.28 | 0.75 | 15 | empty |
| 3 | 55 | 0.26 | 0.73 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4W7W · High-resolution structure of XacCel5A in complex with cellopentaose · 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 Q8PRD3
- Elsewhere: RCSB PDB 4W7W · PDBe 4W7W · UniProt Q8PRD3
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