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Crystal structure of bacillus subtilis ywea

Analyse Crystal structure of bacillus subtilis ywea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MKD
Type
protein
Length
494 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ywea
UniProt
A0A164UMC7
Pockets
2 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CYweaprotein1246% helix, 48% strandA0A164UMC7
DYweaprotein1225% helix, 48% strandA0A164UMC7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19780.690.7467empty
2750.380.7815empty

Interfaces

5 interfaces between chains.

  • A–B · 637 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 635 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 230 Ų buried · 0 hydrogen bonds · protein-protein
  • A–C · 79 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 56 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5MKD · Crystal structure of Bacillus subtilis Ywea · the same entry in another collection · chain A against A, TM-score 1.00

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