› 1iz2

X-ray diffraction
2.2Å resolution

Interactions causing the kinetic trap in serpin protein folding

Released:
DOI: 10.2210/pdb1iz2/pdb
PDB entry 1iz2 coloured by chain, front view.
PDB entry 1iz2 coloured by chain, side view.
PDB entry 1iz2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interactions causing the kinetic trap in serpin protein folding.
Im H, Woo MS, Hwang KY, Yu MH
J Biol Chem 277 46347-54 (2002)
PMID: 12244055

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-133784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-1-antitrypsin Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01009 (Residues: 25-418; Coverage: 100%)
Gene names: AAT, PI, PRO0684, PRO2209, SERPINA1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: Z6W, GLC
Ligand Z6W 1 x Z6W
Ligand GLC 1 x GLC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6B
Spacegroup: P212121
Unit cell:
a: 63.02Å b: 74.173Å c: 93.115Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.211 0.278
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Conformational pathology of the serpins: themes, variations, and therapeutic strategies.
Gooptu et al. (2009)
7 more

15 mentions without citation

Successes and challenges in simulating the folding of large proteins.
Gershenson et al. (2020)
14 more