› 4u7m

X-ray diffraction
2.76Å resolution

LRIG1 extracellular domain: Structure and Function Analysis

Released:
DOI: 10.2210/pdb4u7m/pdb
PDB entry 4u7m coloured by chain, front view.
PDB entry 4u7m coloured by chain, side view.
PDB entry 4u7m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
LRIG1 extracellular domain: structure and function analysis.
Xu Y, Soo P, Walker F, Zhang HH, Redpath N, Tan CW, Nicola NA, Adams TE, Garrett TP, Zhang JG, Burgess AW
J Mol Biol 427 1934-48 (2015)
PMID: 25765764

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine-rich repeats and immunoglobulin-like domains protein 1 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 32.43 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q96JA1 (Residues: 494-781; Coverage: 27%)
Gene names: LIG1, LRIG1
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P43212
Unit cell:
a: 121.04Å b: 121.04Å c: 115.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.253
Expression system: Spodoptera frugiperda

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Citations

1 review citation

HYPOTHESIS: Do LRIG Proteins Regulate Stem Cell Quiescence by Promoting BMP Signaling?
Herdenberg et al. (2023)
6 other articles