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Crystal structure of engineered trifunctional CTCEL5E

Analyse Crystal structure of engineered trifunctional CTCEL5E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5BYW
Type
protein
Length
1,596 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endoglucanase H
EC
3.2.1.4
UniProt
P16218
Pockets
14 · best druggability 0.88

Structure

x-ray diffraction · 5 distinct chains · 44% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndoglucanase H (EC 3.2.1.4)protein31945% helix, 13% strandP16218
BEndoglucanase H (EC 3.2.1.4)protein31645% helix, 13% strandP16218
CEndoglucanase H (EC 3.2.1.4)protein31844% helix, 12% strandP16218
DEndoglucanase H (EC 3.2.1.4)protein32043% helix, 12% strandP16218
EEndoglucanase H (EC 3.2.1.4)protein32343% helix, 12% strandP16218

Pockets

14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17720.880.9176empty
26390.860.9056empty
34920.830.9076empty
410020.770.79112empty
52940.720.8554empty

Interfaces

8 interfaces between chains.

  • A–D · 1420 Ų buried · 20 hydrogen bonds · protein-protein
  • B–E · 1395 Ų buried · 20 hydrogen bonds · protein-protein
  • A–E · 484 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 478 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 474 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5BYW · Crystal structure of engineered trifunctional CtCEL5E · the same entry in another collection · chain E against E, TM-score 1.00
  • P16218 · AlphaFold monomer V2.0 prediction for endoglucanase H (P16218) · a predicted model of the same protein · chain B against A, TM-score 0.96

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