› 1xqg

X-ray diffraction
3.1Å resolution

3.10 A crystal structure of maspin, Space group P 4 21 2

Released:
DOI: 10.2210/pdb1xqg/pdb
PDB entry 1xqg coloured by chain, front view.
PDB entry 1xqg coloured by chain, side view.
PDB entry 1xqg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human maspin, a serpin with antitumor properties: reactive center loop of maspin is exposed but constrained.
Al-Ayyoubi M, Gettins PG, Volz K
J Biol Chem 279 55540-4 (2004)
PMID: 15501821

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-153266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serpin B5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 389 amino acids
Theoretical weight: 43.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P36952 (Residues: 1-375; Coverage: 100%)
Gene names: PI5, SERPINB5
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: APS BEAMLINE 22-ID
Spacegroup: P4212
Unit cell:
a: 147.462Å b: 147.462Å c: 118.038Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.252
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Maspin: molecular mechanisms and therapeutic implications.
Bodenstine et al. (2012)
4 more

4 mentions without citation

Serpin peptidase inhibitor (SERPINB5) haplotypes are associated with susceptibility to hepatocellular carcinoma.
Yang et al. (2016)
3 more