Research workbench
3B' carbohydrate-binding module from the CEL9V glycoside hydrolase from clostridium thermocellum. orthorhombic structure
Analyse 3B' carbohydrate-binding module from the CEL9V glycoside hydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WOB
- Type
- protein
- Length
- 459 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase, family 9
- UniProt
- A3DJ30
- Ligands
- CA
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase, family 9 | protein | 150 | 10% helix, 47% strand | A3DJ30 |
| C | Glycoside hydrolase, family 9 | protein | 153 | 6% helix, 46% strand | A3DJ30 |
| E | Glycoside hydrolase, family 9 | protein | 156 | 10% helix, 44% strand | A3DJ30 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, C, E
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 | 205 | 0.53 | 0.78 | 33 | empty |
| 2 | 214 | 0.50 | 0.76 | 30 | empty |
Interfaces
2 interfaces between chains.
- A–E · 266 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 186 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2WOB · 3b' carbohydrate-binding module from the Cel9V glycoside hydrolase from Clostridium… · 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 A3DJ30
- Elsewhere: RCSB PDB 2WOB · PDBe 2WOB · UniProt A3DJ30
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