Research workbench
Crystal structure of human cadherin-23 EC13-14
Analyse Crystal structure of human cadherin-23 EC13-14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WJ8
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cadherin-23
- UniProt
- Q9H251
- Ligands
- CA, K, CL
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cadherin-23 | protein | 210 | 6% helix, 47% strand | Q9H251 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 5WJ8 · Crystal Structure of Human Cadherin-23 EC13-14 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9H251
- Elsewhere: RCSB PDB 5WJ8 · PDBe 5WJ8 · UniProt Q9H251
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