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Structure of hewl by electron diffraction and microfocus diffraction

Analyse Structure of hewl by electron diffraction and microfocus diffraction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HT2
Type
protein
Length
258 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysozyme C
EC
3.2.1.17
UniProt
P00698
Ligands
CL
Pockets
2 · best druggability 0.62

Structure

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

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

Ligands and binding sites

  • CL · Chloride ion · ion · 19 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14040.620.7738CL
2770.350.7616empty

Interfaces

1 interface between chains.

  • A–B · 289 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 6HT2 · Structure of hewl by electron diffraction and microfocus diffraction · the same entry in another collection · chain A against A, TM-score 1.00

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