MolNFT v1 · #5198 · protein
Dimeric structure of the coxsackie virus and adenovirus receptor D1 domain at 1.35 ångström resolution
1EAJ: “Dimeric structure of the coxsackie virus and adenovirus receptor D1 domain at 1.35 ångström resolution”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.62). MolNFT v1 #5198 on GenesisL1: 3D structure, binding sites…
- 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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