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Structure of Kluyveromyces marxianus Usb1

Analyse Structure of Kluyveromyces marxianus Usb1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PFQ
Type
protein
Length
640 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.8
Source
Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275)
Molecule
Uncharacterized protein YLR132C
UniProt
W0TCJ5
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · resolution 1.8 · 3 distinct chains · 39% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CUncharacterized protein YLR132Cprotein21240% helix, 29% strandW0TCJ5
AUncharacterized protein YLR132Cprotein21639% helix, 28% strandW0TCJ5
BUncharacterized protein YLR132Cprotein21237% helix, 29% strandW0TCJ5

Ligands and binding sites

  • GOL · Glycerol · additive · 11 copies · chains C, A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111500.740.77104GOL
22910.590.7826GOL
32820.570.7727GOL
41650.520.7922GOL
51080.450.7928empty

Interfaces

3 interfaces between chains.

  • C–A · 740 Ų buried · 9 hydrogen bonds · protein-protein
  • C–B · 323 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 175 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6PFQ · Structure of kluyveromyces marxianus USB1 · the same entry in another collection · chain A against A, TM-score 1.00

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