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Laboratory evolved variant R-C1B1D33E6 of potato epoxide hydrolase STEH1

Analyse Laboratory evolved variant R-C1B1D33E6 of potato epoxide hydrolase STEH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4UFO
Type
protein
Length
641 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Epoxide hydrolase
EC
3.3.2.3
UniProt
Q41415
Pockets
4 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEpoxide hydrolase (EC 3.3.2.3)protein32144% helix, 16% strandQ41415
BEpoxide hydrolase (EC 3.3.2.3)protein32044% helix, 16% strandQ41415

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15950.820.8767empty
25020.820.8861empty
34380.660.7854empty
4510.310.7611empty

Interfaces

1 interface between chains.

  • A–B · 562 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4UFO · Laboratory evolved variant R-C1B1D33E6 of potato epoxide hydrolase StEH1 · the same entry in another collection · chain A against A, TM-score 1.00

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