› 1erh

Solution NMR

THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE EXTRACELLULAR REGION OF THE COMPLEMENT REGULATORY PROTEIN, CD59, A NEW CELL SURFACE PROTEIN DOMAIN RELATED TO NEUROTOXINS

Released:
DOI: 10.2210/pdb1erh/pdb
PDB entry 1erh coloured by chain, ensemble of 10 models, front view.
PDB entry 1erh coloured by chain, ensemble of 10 models, side view.
PDB entry 1erh coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins.
Kieffer B, Driscoll PC, Campbell ID, Willis AC, van der Merwe PA, Davis SJ
Biochemistry 33 4471-82 (1994)
PMID: 7512825

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CD59 glycoprotein Chain: A
Molecule details ›
Chain: A
Length: 70 amino acids
Theoretical weight: 8.1 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P13987 (Residues: 26-95; Coverage: 68%)
Gene names: CD59, MIC11, MIN1, MIN2, MIN3, MSK21
Sequence domains: u-PAR/Ly-6 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

24 review citations

Glycosylation: heterogeneity and the 3D structure of proteins.
Rudd et al. (1997)
23 more

1 mention without citation

High-resolution structures of bacterially expressed soluble human CD59.
Leath et al. (2007)