Research workbench
Protocadherin gamma A4 extracellular cadherin domains 3-6
Analyse Protocadherin gamma A4 extracellular cadherin domains 3-6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SZQ
- Type
- protein
- Length
- 422 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protocadherin gamma-A4
- UniProt
- Q91XY4
- Ligands
- MAN, NAG, CA
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protocadherin gamma-A4 | protein | 422 | 5% helix, 47% strand | Q91XY4 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- CA · Calcium ion · metal · 9 copies · chains A
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 | 57 | 0.65 | 0.93 | 20 | empty |
Modifications
Observed in the structure: 8 glycan (O-glycosylation, N-glycosylation).
Compared structures
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 Q91XY4
- Elsewhere: RCSB PDB 5SZQ · PDBe 5SZQ · UniProt Q91XY4
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