Research workbench
PcdhgB3 EC1-4 in 50 mM HEPES
Analyse PcdhgB3 EC1-4 in 50 mM HEPES in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MEQ
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Homo sapiens
- Molecule
- Protocadherin gamma-B3
- UniProt
- Q9Y5G1
- Ligands
- CA
Structure
x-ray diffraction · resolution 2.9 · 1 distinct chain · 7% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protocadherin gamma-B3 | protein | 416 | 7% helix, 46% strand | Q9Y5G1 |
Ligands and binding sites
- 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: 1 disulfide (disulfide).
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 Q9Y5G1
- Elsewhere: RCSB PDB 6MEQ · PDBe 6MEQ · UniProt Q9Y5G1
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