› 4rtd

X-ray diffraction
3.65Å resolution

Escherichia coli alpha-2-macroglobulin activated by porcine elastase

Released:
DOI: 10.2210/pdb4rtd/pdb
PDB entry 4rtd coloured by chain, front view.
PDB entry 4rtd coloured by chain, side view.
PDB entry 4rtd coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
Fyfe CD, Grinter R, Josts I, Mosbahi K, Roszak AW, Cogdell RJ, Wall DM, Burchmore RJ, Byron O, Walker D
Acta Crystallogr D Biol Crystallogr 71 1478-86 (2015)
PMID: 26143919

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 23 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: R3
Unit cell:
a: 176.065Å b: 176.065Å c: 161.131Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.177 0.238
Expression system: Escherichia coli

Quick links

Citations

2 review citations

CD109 and squamous cell carcinoma.
Qi et al. (2018)
1 more

2 mentions without citation

Structure of protease-cleaved Escherichia coli α-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.
Fyfe et al. (2015)
1 more