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1.67 ångström resolution crystal structure of murein-dd-endopeptidase from yersinia enterocolitica.

Analyse 1.67 ångström resolution crystal structure of murein-dd-endopeptidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6MUQ
Type
protein
Length
267 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Murein-dd-endopeptidase
UniProt
A0A0H3NPR7
Ligands
SO4
Pockets
1 · best druggability 0.26

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMurein-dd-endopeptidaseprotein26736% helix, 24% strandA0A0H3NPR7

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1540.260.7321empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

  • 6MUQ · 1.67 Angstrom Resolution Crystal Structure of Murein-DD-endopeptidase from Yersinia… · the same entry in another collection · chain A against A, TM-score 1.00

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