› 2arq

X-ray diffraction
1.85Å resolution

Human plasminogen activator inhibitor-2.[loop (66-98) deletion mutant] complexed with peptide n-acetyl-teaaagdggvmtgr-oh

Released:
DOI: 10.2210/pdb2arq/pdb
PDB entry 2arq coloured by chain, front view.
PDB entry 2arq coloured by chain, side view.
PDB entry 2arq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Plasminogen activator inhibitor-2 is highly tolerant to P8 residue substitution--implications for serpin mechanistic model and prediction of nsSNP activities.
Di Giusto DA, Sutherland AP, Jankova L, Harrop SJ, Curmi PM, King GC
J Mol Biol 353 1069-80 (2005)
PMID: 16214170

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138522 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Plasminogen activator inhibitor 2 Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 42.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05120 (Residues: 1-415; Coverage: 92%)
Gene names: PAI2, PLANH2, SERPINB2
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Plasminogen activator inhibitor 2 Chain: P
Molecule details ›
Chain: P
Length: 15 amino acids
Theoretical weight: 1.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05120 (Residues: 367-380; Coverage: 3%)
Gene names: PAI2, PLANH2, SERPINB2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P21212
Unit cell:
a: 92.562Å b: 104.126Å c: 41.438Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.248
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Stability of domain structures in multi-domain proteins.
Bhaskara et al. (2011)
2 more

1 mention without citation

Dependence on endocytic receptor binding via a minimal binding motif underlies the differential prognostic profiles of SerpinE1 and SerpinB2 in cancer.
Cochran et al. (2011)