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Laboratory evolved variant R-C1B1D33 of potato epoxide hydrolase STEH1

Analyse Laboratory evolved variant R-C1B1D33 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
4UFP
Type
protein
Length
638 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 0.81

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BEpoxide hydrolase (EC 3.3.2.3)protein31943% helix, 17% strandQ41415

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14680.810.8759empty
25930.800.8566empty
33810.630.7850empty
4520.280.7518empty

Interfaces

1 interface between chains.

  • A–B · 590 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4UFP · Laboratory evolved variant R-C1B1D33 of potato epoxide hydrolase StEH1 · the same entry in another collection · chain A against A, TM-score 1.00

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