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Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8

Analyse Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UC8
Type
protein
Length
505 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Thermus thermophilus
Molecule
lysine biosynthesis enzyme
Pockets
3 · best druggability 0.56

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 39% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Alysine biosynthesis enzymeprotein25439% helix, 26% strand—
Blysine biosynthesis enzymeprotein25139% helix, 26% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12510.560.7831empty
21010.400.7719empty
31000.380.7616empty

Interfaces

1 interface between chains.

  • A–B · 1903 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 1UC8 · Crystal structure of a lysine biosynthesis enzyme, lysx, from thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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