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Endoglucanase CEL5G from pseudoalteromonas haloplanktis in complex with cellobiose

Analyse Endoglucanase CEL5G from pseudoalteromonas haloplanktis in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TVP
Type
protein
Length
584 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cellulase
EC
3.2.1.4
UniProt
O86099
Ligands
BGC
Pockets
3 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACellulase (EC 3.2.1.4)protein29339% helix, 20% strandO86099
BCellulase (EC 3.2.1.4)protein29138% helix, 21% strandO86099

Ligands and binding sites

  • BGC · beta-D-glucopyranose · sugar · 2 copies · chains B
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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
14950.760.8458EPE
21100.410.7618empty
31070.400.7618BGC

Interfaces

1 interface between chains.

  • A–B · 706 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 1TVP · Endoglucanase cel5G from Pseudoalteromonas haloplanktis in complex with cellobiose · the same entry in another collection · chain A against A, TM-score 1.00

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