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Structural effects of monovalent anions on polymorphic lysozyme crystals

Analyse Structural effects of monovalent anions on polymorphic lysozyme crystals in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B2K
Type
protein
Length
258 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (lysozyme)
EC
3.2.1.17
UniProt
P00698
Ligands
IOD
Pockets
3 · best druggability 0.38

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BProtein (lysozyme) (EC 3.2.1.17)protein12941% helix, 11% strandP00698

Ligands and binding sites

  • IOD · Iodide ion · ion · 17 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1920.380.7616empty
2800.350.7515IOD
3630.280.7320IOD

Interfaces

1 interface between chains.

  • A–B · 300 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 1B2K · Structural effects of monovalent anions on polymorphic lysozyme crystals · the same entry in another collection · chain A against A, TM-score 1.00

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