Research workbench
Rhinovirus C15 complexed with domains I and II of receptor CDHR3
Analyse Rhinovirus C15 complexed with domains I and II of receptor CDHR3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PSF
- Type
- protein
- Length
- 882 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E5D8F2, Q6ZTQ4
Structure
electron microscopy · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 261 | — | E5D8F2 |
| B | — | protein | 235 | — | E5D8F2 |
| C | — | protein | 253 | — | E5D8F2 |
| D | — | protein | 25 | — | E5D8F2 |
| U | — | protein | 108 | — | Q6ZTQ4 |
Compared structures
- 6PSF · Rhinovirus C15 complexed with domains I and II of receptor CDHR3 · the same entry in another collection · chain A against A, TM-score 1.00
- Q6ZTQ4 · AlphaFold monomer V2.0 prediction for cadherin-related family member 3 (Q6ZTQ4) · a predicted model of the same protein · chain U against A, TM-score 0.94
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 E5D8F2
- Every structure of UniProt Q6ZTQ4
- Elsewhere: RCSB PDB 6PSF · PDBe 6PSF · UniProt E5D8F2 · UniProt Q6ZTQ4
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