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Crystal structure of the extracellular domains of coxsackie & adenovirus receptor from mouse (mcar)
Analyse Crystal structure of the extracellular domains of coxsackie & adenovirus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JZ7
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coxsackievirus and adenovirus receptor homolog
- UniProt
- P97792
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coxsackievirus and adenovirus receptor homolog | protein | 209 | 9% helix, 47% strand | P97792 |
Ligands and binding sites
- IPA · Isopropyl alcohol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3JZ7 · Crystal structure of the extracellular domains of coxsackie & adenovirus receptor from… · the same entry in another collection · chain A against A, TM-score 1.00
- P97792 · AlphaFold monomer V2.0 prediction for coxsackievirus and adenovirus receptor homolog… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P97792
- Elsewhere: RCSB PDB 3JZ7 · PDBe 3JZ7 · UniProt P97792
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