› 1c1z

X-ray diffraction
2.87Å resolution

CRYSTAL STRUCTURE OF HUMAN BETA-2-GLYCOPROTEIN-I (APOLIPOPROTEIN-H)

Released:
DOI: 10.2210/pdb1c1z/pdb
PDB entry 1c1z coloured by chain, front view.
PDB entry 1c1z coloured by chain, side view.
PDB entry 1c1z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome.
Schwarzenbacher R, Zeth K, Diederichs K, Gries A, Kostner GM, Laggner P, Prassl R
EMBO J 18 6228-39 (1999)
PMID: 10562535

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136130 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Beta-2-glycoprotein 1 Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 36.31 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02749 (Residues: 20-345; Coverage: 100%)
Gene names: APOH, B2G1
Sequence domains:
Structure domains: Complement Module, domain 1

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, NDG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, NDG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2221
Unit cell:
a: 159.5Å b: 164.8Å c: 114.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.238 0.244

Quick links

Citations

60 review citations

The pathogenesis of the antiphospholipid syndrome.
Giannakopoulos et al. (2013)
59 more

23 mentions without citation

Control of blood proteins by functional disulfide bonds.
Butera et al. (2014)
22 more