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Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability

Analyse Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1LWK
Type
protein
Length
162 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysozyme
EC
3.2.1.17
UniProt
P00720
Ligands
CL
Pockets
2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALysozyme (EC 3.2.1.17)protein16266% helix, 7% strandP00720

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A
  • HED · 2-hydroxyethyl disulfide · additive · chains A

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
13150.630.7936empty
2870.420.7915empty

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

  • 1LWK · Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects… · the same entry in another collection · chain A against A, TM-score 1.00

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