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Crystal structure of the endo-1,4-glucanase RBcel1 E135A with cellotriose

Analyse Crystal structure of the endo-1,4-glucanase RBcel1 E135A with cellotriose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LJF
Type
protein
Length
638 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.7344
Source
uncultured bacterium
Molecule
Endoglucanase
EC
3.2.1.4
UniProt
C1JI15
Ligands
BGC
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · resolution 1.7344 · 2 distinct chains · 36% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndoglucanase (EC 3.2.1.4)protein32136% helix, 16% strandC1JI15
BEndoglucanase (EC 3.2.1.4)protein31736% helix, 16% strandC1JI15

Ligands and binding sites

  • BGC · beta-D-glucopyranose · sugar · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110770.780.8085BGC
22040.500.7635BGC
3780.330.7520empty

Interfaces

1 interface between chains.

  • A–B · 554 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 5LJF · Crystal structure of the endo-1,4-glucanase RBCEL1 E135A with cellotriose · the same entry in another collection · chain A against A, TM-score 1.00

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