MolNFT v2 · #198029 · protein
Crystal structure of human coronavirus 229E spike protein receptor-binding domain in complex with C04 Fab
7VN9: “Crystal structure of human coronavirus 229E spike protein receptor-binding domain in complex with C04 Fab”. X-ray diffraction at 4.49, 2 ligands (NAG, BMA). MolNFT v2 #198029 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7VN9
- Type
- protein
- Length
- 1,113 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.49
- Source
- Homo sapiens; Human coronavirus 229E
- UniProt
- P15423
- Ligands
- NAG, BMA
Structure
x-ray diffraction · resolution 4.49 · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | — | protein | 218 | — | — |
| L | — | protein | 213 | — | — |
| E | — | protein | 134 | — | P15423 |
| A | — | protein | 215 | — | — |
| B | — | protein | 198 | — | — |
| C | — | protein | 135 | — | P15423 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains E, H, C
- BMA · beta-D-mannopyranose · sugar · 2 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P15423
- Elsewhere: RCSB PDB 7VN9 · PDBe 7VN9 · UniProt P15423
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