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Crystal structure of an alkyl hyroperoxide reductase from burkholderia ambifaria

Analyse Crystal structure of an alkyl hyroperoxide reductase from burkholderia ambifaria in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ENU
Type
protein
Length
310 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alkyl hydroperoxide reductase/ thiol specific antioxidant/ mal allergen
UniProt
B1YRI5
Pockets
1 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlkyl hydroperoxide reductase/ thiol specific antioxidant/ mal allergenprotein15732% helix, 29% strandB1YRI5
BAlkyl hydroperoxide reductase/ thiol specific antioxidant/ mal allergenprotein15333% helix, 30% strandB1YRI5

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.470.7927empty

Interfaces

1 interface between chains.

  • A–B · 442 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 5ENU · Crystal structure of an alkyl hyroperoxide reductase from Burkholderia ambifaria · the same entry in another collection · chain A against A, TM-score 1.00

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