Research workbench
Protocadherin gamma A8 extracellular cadherin domains 1-4
Analyse Protocadherin gamma A8 extracellular cadherin domains 1-4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SZM
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PCDHGA8 or protocadherin gamma A8
- UniProt
- Q91XY0
- Ligands
- NAG, MAN, BMA, FUC, CA
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PCDHGA8 or protocadherin gamma A8 | protein | 416 | 7% helix, 45% strand | Q91XY0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · 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.
Modifications
Observed in the structure: 4 glycan, 1 disulfide (N-glycosylation, O-glycosylation, disulfide).
Compared structures
- 5SZM · Protocadherin gamma A8 extracellular cadherin domains 1-4 · 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 Q91XY0
- Elsewhere: RCSB PDB 5SZM · PDBe 5SZM · UniProt Q91XY0
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