› 1dvm

X-ray diffraction
2.4Å resolution

ACTIVE FORM OF HUMAN PAI-1

Released:
DOI: 10.2210/pdb1dvm/pdb
PDB entry 1dvm coloured by chain, front view.
PDB entry 1dvm coloured by chain, side view.
PDB entry 1dvm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of active and latent PAI-1: a possible stabilizing role for chloride ions.
Stout TJ, Graham H, Buckley DI, Matthews DJ
Biochemistry 39 8460-9 (2000)
PMID: 10913251

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-138523 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plasminogen activator inhibitor 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 379 amino acids
Theoretical weight: 42.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05121 (Residues: 24-402; Coverage: 100%)
Gene names: PAI1, PLANH1, SERPINE1
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P1
Unit cell:
a: 64.764Å b: 74.674Å c: 103.445Å
α: 85.19° β: 86.17° γ: 64.34°
R-values:
R R work R free
0.214 0.218 0.292
Expression system: Escherichia coli

Quick links

Citations

10 review citations

An overview of the serpin superfamily.
Law et al. (2006)
9 more

12 mentions without citation

Targeting PAI-1 in Cardiovascular Disease: Structural Insights Into PAI-1 Functionality and Inhibition.
Sillen et al. (2020)
11 more