Research workbench
Structural basis for variation in adenovirus affinity for the cellular receptor car (P417S mutant)
Analyse Structural basis for variation in adenovirus affinity for the cellular receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P69
- Type
- protein
- Length
- 309 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P36711, P78310
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | P36711 |
| B | — | protein | 124 | — | P78310 |
Compared structures
- 1P69 · Structural basis for variation in adenovirus affinity for the cellular receptor car… · the same entry in another collection · chain A against A, TM-score 1.00
- P78310 · AlphaFold monomer V2.0 prediction for coxsackievirus and adenovirus receptor (P78310) · a predicted model of the same protein · chain B 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 P36711
- Every structure of UniProt P78310
- Elsewhere: RCSB PDB 1P69 · PDBe 1P69 · UniProt P36711 · UniProt P78310
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