Research workbench

Laboratory evolved variant R-C1B1 of potato epoxide hydrolase STEH1

Analyse Laboratory evolved variant R-C1B1 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: 4UFN
Type: protein
Length: 640 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: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Epoxide hydrolase (EC 3.3.2.3)	protein	320	44% helix, 16% strand	Q41415

Ligands and binding sites

DIO · 1,4-diethylene dioxide · additive · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.81	0.88	64	DIO
2	477	0.77	0.85	58	DIO
3	429	0.65	0.78	58	empty

Interfaces

1 interface between chains.

A–B · 565 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4UFN · Laboratory evolved variant R-C1B1 of potato epoxide hydrolase StEH1 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q41415
Elsewhere: RCSB PDB 4UFN · PDBe 4UFN · UniProt Q41415

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