MolNFT v2 · #158440 · protein
CryoEM structure of chimeric Eastern Equine Encephalitis Virus
6MX4: “CryoEM structure of chimeric Eastern Equine Encephalitis Virus”. Electron microscopy at 4.4, 1 ligand (NAG). MolNFT v2 #158440 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6MX4
- Type
- protein
- Length
- 4,039 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.4
- Source
- Eastern equine encephalitis virus
- UniProt
- E9KXM2, E9KXL2, P27284
- Ligands
- NAG
Structure
electron microscopy · resolution 4.4 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | — | protein | 430 | — | E9KXM2 |
| B, E, H, K | — | protein | 420 | — | E9KXL2 |
| C, I, L | — | protein | 160 | — | P27284 |
| F | — | protein | 159 | — | P27284 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A, D, G, J, B, E, H, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MX4 · Cryoem structure of chimeric eastern equine encephalitis virus · 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 E9KXM2
- Every structure of UniProt E9KXL2
- Every structure of UniProt P27284
- Elsewhere: RCSB PDB 6MX4 · PDBe 6MX4 · UniProt E9KXM2 · UniProt E9KXL2 · UniProt P27284
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