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Crystal structure of the bacterial lysozyme from streptomyces coelicolor at 1.65 a resolution

Analyse Crystal structure of the bacterial lysozyme from streptomyces coelicolor at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1JFX
Type
protein
Length
217 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
1,4-beta-N-acetylmuramidase M1
EC
3.2.1.17
UniProt
P25310
Ligands
CL
Pockets
2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A1,4-beta-N-acetylmuramidase M1 (EC 3.2.1.17)protein21730% helix, 25% strandP25310

Ligands and binding sites

  • CL · Chloride ion · ion · 8 copies · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1850.370.7622empty
2860.360.7619CL

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1JFX · Crystal structure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A… · the same entry in another collection · chain A against A, TM-score 1.00
  • P25310 · AlphaFold monomer V2.0 prediction for lysozyme M1 (P25310) · a predicted model of the same protein · chain A against A, TM-score 0.99

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