Research workbench
X-ray crystal structure of a non-crystalline cellulose specific carbohydrate-binding module: CBM28.
Analyse X-ray crystal structure of a non-crystalline cellulose specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UWW
- Type
- protein
- Length
- 363 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- P06564
- Ligands
- CA
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase (EC 3.2.1.4) | protein | 184 | 5% helix, 44% strand | P06564 |
| B | Endoglucanase (EC 3.2.1.4) | protein | 179 | 5% helix, 46% strand | P06564 |
Ligands and binding sites
- CA · Calcium ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.67 | 0.95 | 17 | empty |
| 2 | 228 | 0.60 | 0.80 | 31 | empty |
| 3 | 280 | 0.56 | 0.77 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 948 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1UWW · X-ray crystal structure of a non-crystalline cellulose specific carbohydrate-binding… · the same entry in another collection · chain A against A, TM-score 1.00
- P06564 · AlphaFold monomer V2.0 prediction for endoglucanase (P06564) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P06564
- Elsewhere: RCSB PDB 1UWW · PDBe 1UWW · UniProt P06564
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