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Structure of muramidase from acremonium alcalophilum

Analyse Structure of muramidase from acremonium alcalophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZM8
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Muramidase
EC
3.2.1.17
Pockets
2 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMuramidase (EC 3.2.1.17)protein20830% helix, 22% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.370.7421empty
21000.370.7521empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 6ZM8 · Structure of muramidase from Acremonium alcalophilum · the same entry in another collection · chain A against A, TM-score 1.00

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