MolNFT v1 · #174856 · protein
Structural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2
7C8K: “Structural basis for cross-species recognition of COVID-19 virus spike receptor binding domain to bat ACE2”. Electron microscopy, 2 ligands (NAG, ZN). MolNFT v1 #174856 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7C8K
- Type
- protein
- Length
- 596 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E2DHI3
- Ligands
- NAG, ZN
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 596 | — | E2DHI3 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7C8K · Structural basis for cross-species recognition of COVID-19 virus spike receptor binding… · 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 E2DHI3
- Elsewhere: RCSB PDB 7C8K · PDBe 7C8K · UniProt E2DHI3
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