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Unusual structural features in the adduct of dirhodium tetraacetate with lysozyme (5)

Analyse Unusual structural features in the adduct of dirhodium tetraacetate with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BEC
Type
protein
Length
129 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.74
Source
Gallus gallus
Molecule
Lysozyme
EC
3.2.1.17
UniProt
P00698
Ligands
RH, NA, NO3
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · resolution 1.74 · 1 distinct chain · 41% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAALysozyme (EC 3.2.1.17)protein12941% helix, 11% strandP00698

Ligands and binding sites

  • RH · Rhodium · metal · 3 copies · chains AAA
  • NA · Sodium ion · metal · chains AAA
  • NO3 · Nitrate ion · ion · 5 copies · chains AAA
  • ACT · Acetate ion · additive · 2 copies · chains AAA
  • EDO · 1,2-ethanediol · additive · chains AAA

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
1640.340.7616NO3

Modifications

Observed in the structure: 4 disulfide (disulfide).

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