Research workbench
Crystal structure of the BLCEL48B from bacillus licheniformis
Analyse Crystal structure of the BLCEL48B from bacillus licheniformis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KW6
- Type
- protein
- Length
- 697 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exoglucanase-2
- UniProt
- A0A6I7VUD0
- Ligands
- BGC, CA
- Pockets
- 1 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exoglucanase-2 | protein | 697 | 37% helix, 18% strand | A0A6I7VUD0 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 6 copies · chains A
- CA · Calcium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 12 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1123 | 0.86 | 0.87 | 94 | BGC, EDO |
Compared structures
- 7KW6 · Crystal structure of the BlCel48B from Bacillus licheniformis · 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 A0A6I7VUD0
- Elsewhere: RCSB PDB 7KW6 · PDBe 7KW6 · UniProt A0A6I7VUD0
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