MolNFT v1 · #157382 · protein
Cryoem structure of chimeric eastern equine encephalitis virus
6MX4: “Cryoem structure of chimeric eastern equine encephalitis virus”. Electron microscopy, 1 ligand (NAG). MolNFT v1 #157382 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 v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E9KXM2, E9KXL2, P27284
- Ligands
- NAG
Structure
electron microscopy · 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 G against G, 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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