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The crystal structure of epoxide hydrolase B (RV1938) from mycobacterium tuberculosis at 2.1 ångström

Analyse The crystal structure of epoxide hydrolase B (RV1938) from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2E3J
Type: protein
Length: 346 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epoxide hydrolase ephb
EC: 3.3.2.3
UniProt: P95276
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epoxide hydrolase ephb (EC 3.3.2.3)	protein	346	45% helix, 16% strand	P95276

Ligands and binding sites

ACT · Acetate ion · additive · 9 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.74	0.97	20	ACT
2	145	0.48	0.77	23	empty

Compared structures

2E3J · The crystal structure of epoxide hydrolase B (Rv1938) from mycobacterium tuberculosis at… · the same entry in another collection · chain A against A, TM-score 1.00
P95276 · AlphaFold monomer V2.0 prediction for epoxide hydrolase B (P95276) · a predicted model of the same protein · 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 P95276
Elsewhere: RCSB PDB 2E3J · PDBe 2E3J · UniProt P95276

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