› 5x4r

X-ray diffraction
1.5Å resolution

Structure of the N-terminal domain (NTD) of MERS-CoV spike protein

Released:
DOI: 10.2210/pdb5x4r/pdb
PDB entry 5x4r coloured by chain, front view.
PDB entry 5x4r coloured by chain, side view.
PDB entry 5x4r coloured by chain, top view.
Source organism: Middle East respiratory syndrome-related coronavirus
Primary publication:
Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.
Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF
Nat Commun 8 15092 (2017)
PMID: 28393837

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-125661 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Spike protein S1 Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 38.55 KDa
Source organism: Middle East respiratory syndrome-related coronavirus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: K9N5Q8 (Residues: 18-353; Coverage: 25%)
Gene names: 3, S
Sequence domains: Betacoronavirus-like spike glycoprotein S1, N-terminal

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 51.615Å b: 86.609Å c: 88.098Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.162 0.195
Expression system: Trichoplusia ni

Quick links

Citations

149 review citations

Origin and evolution of pathogenic coronaviruses.
Cui et al. (2019)
148 more

5 mentions without citation

Human coronavirus spike protein-host receptor recognition.
Guruprasad L. (2020)
4 more