› 2h4p

X-ray diffraction
1.7Å resolution

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-130726 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heterochromatin-associated protein MENT Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 45.27 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O73790 (Residues: 1-369; Coverage: 90%)
Gene names: MENT, SERPINB10
Sequence domains: Serpin (serine protease inhibitor)
Structure domains:
Heterochromatin-associated protein MENT Chain: B
Molecule details ›
Chain: B
Length: 34 amino acids
Theoretical weight: 4.19 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O73790 (Residues: 377-410; Coverage: 8%)
Gene names: MENT, SERPINB10

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P1
Unit cell:
a: 46.486Å b: 47.526Å c: 57.794Å
α: 96.89° β: 93.81° γ: 116.65°
R-values:
R R work R free
0.192 0.191 0.214
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

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

1 mention without citation

X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation.
McGowan et al. (2006)