PDBe 4m6d

X-ray diffraction
2.68Å resolution

Crystal structure of the aptamer minF-lysozyme complex.

Released:
Entry authors: Malashkevich VN, Padlan FC, Toro R, Girvin M, Almo SC, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl- D-glucosamine residues in chitodextrins. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Lysozyme C Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
aptamer Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 45 nucleotides
Theoretical weight: 14.52 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 43.914Å b: 132.289Å c: 131.539Å
α: 118.59° β: 96.39° γ: 96.27°
R-values:
R R work R free
0.168 0.165 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided