Research workbench
Calcium activated chloride channel regulator 1 (CLCA1) vwa domain
Analyse Calcium activated chloride channel regulator 1 (CLCA1) vwa domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PYX
- Type
- protein
- Length
- 320 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cdna FLJ56608, highly similar to homo sapiens chloride channel, calcium activated, family…
- UniProt
- B4DUZ6
- Ligands
- CA
- Pockets
- 2 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cdna FLJ56608, highly similar to homo sapiens chloride channel, calcium activated, family member 1 (CLCA1), mRNA | protein | 163 | 39% helix, 23% strand | B4DUZ6 |
| B | Cdna FLJ56608, highly similar to homo sapiens chloride channel, calcium activated, family member 1 (CLCA1), mRNA | protein | 157 | 39% helix, 24% strand | B4DUZ6 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.45 | 0.75 | 25 | empty |
| 2 | 90 | 0.37 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 522 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6PYX · Calcium Activated Chloride Channel Regulator 1 (CLCA1) VWA Domain · 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 B4DUZ6
- Elsewhere: RCSB PDB 6PYX · PDBe 6PYX · UniProt B4DUZ6
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