Research workbench
Dimeric structure of the coxsackie virus and adenovirus receptor D1 domain at 1.35 ångström resolution
Analyse Dimeric structure of the coxsackie virus and adenovirus receptor D1 domain at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EAJ
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coxsackie virus and adenovirus receptor
- UniProt
- P78310
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coxsackie virus and adenovirus receptor | protein | 124 | 5% helix, 50% strand | P78310 |
| B | Coxsackie virus and adenovirus receptor | protein | 120 | 5% helix, 51% strand | P78310 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.62 | 0.81 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 748 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1EAJ · Dimeric structure of the coxsackie virus and adenovirus receptor D1 domain at 1.35… · 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 0.95
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 P78310
- Elsewhere: RCSB PDB 1EAJ · PDBe 1EAJ · UniProt P78310
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