› 7ymv

Electron Microscopy
6.74Å resolution

Cryo-EM structure of MERS-CoV spike protein, Two RBD-up conformation 1

Released:
DOI: 10.2210/pdb7ymv/pdb
PDB entry 7ymv coloured by chain, front view.
PDB entry 7ymv coloured by chain, side view.
PDB entry 7ymv coloured by chain, top view.
Source organism: Human betacoronavirus 2c EMC/2012
Primary publication:
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries.
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
Cell 187 1296-1311.e26 (2024)
PMID: 38428397
Related structures: EMD-33943

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125457 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (7 distinct):
Spike glycoprotein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 1369 amino acids
Theoretical weight: 150.65 KDa
Source organism: Human betacoronavirus 2c EMC/2012
Expression system: Homo sapiens
UniProt:
  • Canonical: K0BRG7 (Residues: 17-1291; Coverage: 94%)
Gene name: S
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
1 bound ligand:
Ligand NAG 14 x NAG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this EM entry.
Resolution: 6.74Å
Relevant EMDB volumes: EMD-33943
Expression system: Homo sapiens

Quick links

Citations

1 citations in other articles

A curated rotamer library for common post-translational modifications of proteins.
Zhang et al. (2024)