Research workbench
CBM4 structure and function
Analyse CBM4 structure and function in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GUI
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Laminarinase 16A
- UniProt
- Q9WXN1
- Ligands
- BGC, CA
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Laminarinase 16A | protein | 155 | 5% helix, 52% strand | Q9WXN1 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 6 copies · chains A
- CA · Calcium ion · metal · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.32 | 0.74 | 15 | BGC |
Compared structures
- 1GUI · CBM4 structure and function · 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 Q9WXN1
- Elsewhere: RCSB PDB 1GUI · PDBe 1GUI · UniProt Q9WXN1
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