› 3drm

X-ray diffraction
2.2Å resolution

2.2 Angstrom Crystal Structure of Thr114Phe Alpha1-Antitrypsin

Released:
DOI: 10.2210/pdb3drm/pdb
PDB entry 3drm coloured by chain, front view.
PDB entry 3drm coloured by chain, side view.
PDB entry 3drm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: implications for disease and drug design.
Gooptu B, Miranda E, Nobeli I, Mallya M, Purkiss A, Brown SC, Summers C, Phillips RL, Lomas DA, Barrett TE
J Mol Biol 387 857-68 (2009)
PMID: 19232354

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 404 amino acids
Theoretical weight: 45.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 26-418; Coverage: 100%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2
Unit cell:
a: 113.849Å b: 39.63Å c: 90.251Å
α: 90° β: 105.11° γ: 90°
R-values:
R R work R free
0.224 0.224 0.272
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The molecular and cellular pathology of α₁-antitrypsin deficiency.
Gooptu et al. (2014)
3 more

2 mentions without citation

Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: implications for disease and drug design.
Gooptu et al. (2009)
1 more