MolNFT v2 · #150396 · protein
C-terminal domain of MERS-CoV nucleocapsid
6G13: “C-terminal domain of MERS-CoV nucleocapsid”. X-ray diffraction at 1.97, 2 ligands (TMO, CL). MolNFT v2 #150396 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6G13
- Type
- protein
- Length
- 452 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.97
- Source
- Middle East respiratory syndrome-related coronavirus
- UniProt
- A0A0D3MU51
- Ligands
- TMO, CL
Structure
x-ray diffraction · resolution 1.97 · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 112 | — | A0A0D3MU51 |
| B, C | — | protein | 113 | — | A0A0D3MU51 |
| D | — | protein | 114 | — | A0A0D3MU51 |
Ligands and binding sites
- TMO · trimethylamine oxide · ligand · 4 copies · chains A, B, C
- CL · Chloride ion · ion · chains B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6G13 · C-terminal domain of MERS-cov nucleocapsid · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A0D3MU51
- Elsewhere: RCSB PDB 6G13 · PDBe 6G13 · UniProt A0A0D3MU51
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