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Structure of an H300N mutant of potato epoxide hydrolase, STEH1

Analyse Structure of an H300N mutant 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
4Y9S
Type
protein
Length
639 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Epoxide hydrolase
UniProt
Q41415
Pockets
4 · best druggability 0.79

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AEpoxide hydrolaseprotein32044% helix, 16% strandQ41415
BEpoxide hydrolaseprotein31945% helix, 16% strandQ41415

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15210.790.8551empty
24320.780.8643empty
3510.680.9716empty
44280.650.7855empty

Interfaces

1 interface between chains.

  • A–B · 575 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4Y9S · structure of an H300N mutant of potato epoxide hydrolase, StEH1 · the same entry in another collection · chain A against A, TM-score 1.00

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