› 2p9r

X-ray diffraction
2.3Å resolution

Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3

Released:
DOI: 10.2210/pdb2p9r/pdb
PDB entry 2p9r coloured by chain, front view.
PDB entry 2p9r coloured by chain, side view.
PDB entry 2p9r coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3.
Doan N, Gettins PG
Biochem J 407 23-30 (2007)
PMID: 17608619

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133819 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-2-macroglobulin Chains: A, B
Molecule details ›
Chains: A, B
Length: 102 amino acids
Theoretical weight: 11.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01023 (Residues: 126-227; Coverage: 7%)
Gene names: A2M, CPAMD5, FWP007
Sequence domains: MG2 domain
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P43212
Unit cell:
a: 68.81Å b: 68.81Å c: 120.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.244 0.281
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.
Korkmaz et al. (2010)
5 more

4 mentions without citation

Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes.
Frandsen et al. (2016)
3 more