Research workbench
Structure of mouse BAI1 (ADGRB1) TSR3 domain
Analyse Structure of mouse BAI1 (ADGRB1) TSR3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R85
- Type
- protein
- Length
- 44 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vasculostatin-120
- UniProt
- Q3UHD1
- Ligands
- MAN, FUC, BGC
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vasculostatin-120 | protein | 44 | 0% helix, 36% strand | Q3UHD1 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 3 glycan (disulfide, C-mannosylation, O-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 Q3UHD1
- Elsewhere: RCSB PDB 7R85 · PDBe 7R85 · UniProt Q3UHD1
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