› 4csy

X-ray diffraction
2.41Å resolution

E-selectin lectin, EGF-like and two SCR domains complexed with Sialyl Lewis X

Released:
DOI: 10.2210/pdb4csy/pdb
PDB entry 4csy coloured by chain, front view.
PDB entry 4csy coloured by chain, side view.
PDB entry 4csy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
E-selectin ligand complexes adopt an extended high-affinity conformation.
Preston RC, Jakob RP, Binder FP, Sager CP, Ernst B, Maier T
J Mol Cell Biol 8 62-72 (2016)
PMID: 26117840

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
E-selectin Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 31.31 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P16581 (Residues: 22-301; Coverage: 48%)
Gene names: ELAM1, SELE
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MAG, GAL, SIA, FUC
Carbohydrate polymer
2 bound ligands:
Ligand NAG 14 x NAG
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 52.29Å b: 58.67Å c: 58.87Å
α: 76.03° β: 86.28° γ: 86.31°
R-values:
R R work R free
0.217 0.215 0.253
Expression system: Cricetulus griseus

Quick links

Citations

8 review citations

Mammalian sugar-binding receptors: known functions and unexplored roles.
Taylor et al. (2019)
7 more

7 mentions without citation

Glycomimetics for the inhibition and modulation of lectins.
Leusmann et al. (2023)
6 more