› 4r0p

X-ray diffraction
1.52Å resolution

Ifqins, an amyloid forming segment from human lysozyme spanning residues 56-61

Released:
DOI: 10.2210/pdb4r0p/pdb
PDB entry 4r0p coloured by chain, front view.
PDB entry 4r0p coloured by chain, side view.
PDB entry 4r0p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-based design of functional amyloid materials.
Li D, Jones EM, Sawaya MR, Furukawa H, Luo F, Ivanova M, Sievers SA, Wang W, Yaghi OM, Liu C, Eisenberg DS
J Am Chem Soc 136 18044-51 (2014)
PMID: 25474758

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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158308 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 6 amino acids
Theoretical weight: 721 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61626 (Residues: 74-79; Coverage: 5%)
Gene names: LYZ, LZM

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID13
Spacegroup: P212121
Unit cell:
a: 19.607Å b: 4.839Å c: 43.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.158 0.201
Expression system: Not provided

Quick links

Citations

4 review citations

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.
Wei et al. (2017)
3 more

3 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
2 more