› 4wnd

X-ray diffraction
1.5Å resolution

Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 1.5 Angstrom resolution

Released:
DOI: 10.2210/pdb4wnd/pdb
PDB 4wnd coloured by chain and viewed from the front.
PDB 4wnd coloured by chain and viewed from the side.
PDB 4wnd coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN.
Takayanagi H, Yuzawa S, Sumimoto H
Acta Crystallogr F Struct Biol Commun 71 175-83 (2015)
PMID: 25664792

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
G-protein-signaling modulator 2 Chain: A
Molecule details ›
Chain: A
Length: 406 amino acids
Theoretical weight: 44.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P81274 (Residues: 20-421; Coverage: 59%)
Gene names: GPSM2, LGN
Sequence domains:
Structure domains: Tetratricopeptide repeat domain
FERM and PDZ domain-containing protein 4 Chain: B
Molecule details ›
Chain: B
Length: 53 amino acids
Theoretical weight: 5.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q14CM0 (Residues: 978-1025; Coverage: 4%)
Gene names: FRMPD4, KIAA0316, PDZD10, PDZK10

Ligands and Environments

4 bound ligands:
Ligand SCN 7 x SCN
Ligand PEG 5 x PEG
Ligand PGE 1 x PGE
Ligand EDO 6 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 45.487Å b: 64.786Å c: 69.118Å
α: 90° β: 102.33° γ: 90°
R-values:
R R work R free
0.164 0.163 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Molecular mechanism for the regulation of yeast separase by securin.
Luo et al. (2017)
2 more