› 8frr

X-ray diffraction
1.27Å resolution

Wild-type myocilin olfactomedin domain

Released:
DOI: 10.2210/pdb8frr/pdb
PDB entry 8frr coloured by chain, front view.
PDB entry 8frr coloured by chain, side view.
PDB entry 8frr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.
Saccuzzo EG, Mebrat MD, Scelsi HF, Kim M, Ma MT, Su X, Hill SE, Rheaume E, Li R, Torres MP, Gumbart JC, Van Horn WD, Lieberman RL
Nat Commun 15 155 (2024)
PMID: 38168102

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189295 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myocilin, C-terminal fragment Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99972 (Residues: 244-502; Coverage: 55%)
Gene names: GLC1A, MYOC, TIGR
Sequence domains: Olfactomedin-like domain

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand CA 1 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 49.468Å b: 50.527Å c: 50.873Å
α: 90° β: 96.25° γ: 90°
R-values:
R R work R free
0.14 0.14 0.155
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.
Saccuzzo et al. (2024)