GL1X · GenesisL1 explorer

Research workbench

CCCEL6A catalytic domain complexed with cellobiose

Analyse CCCEL6A catalytic domain complexed with cellobiose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VOH
Type
protein
Length
362 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cellobiohydrolase
EC
3.2.1.91
UniProt
B7X9Z0
Ligands
BGC
Pockets
1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACellobiohydrolase (EC 3.2.1.91)protein36239% helix, 12% strandB7X9Z0

Ligands and binding sites

  • BGC · beta-D-glucopyranose · sugar · 6 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13750.730.8452BGC

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3VOH · CcCel6A catalytic domain complexed with cellobiose · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.