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Triclinic lysozyme cryocooled to 100 K with 47% xylose as cryoprotectant

Analyse Triclinic lysozyme cryocooled to 100 K with 47% xylose as cryoprotectant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6D6F
Type
protein
Length
129 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysozyme C
EC
3.2.1.17
UniProt
P00698
Ligands
XYS, NO3
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALysozyme C (EC 3.2.1.17)protein12940% helix, 11% strandP00698

Ligands and binding sites

  • XYS · alpha-D-xylopyranose · sugar · chains A
  • NO3 · Nitrate ion · ion · 7 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.290.7415empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 6D6F · Triclinic lysozyme cryocooled to 100 K with 47% xylose as cryoprotectant · the same entry in another collection · chain A against A, TM-score 1.00

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