Research workbench
N-terminal domain of mouse shisa 3
Analyse N-terminal domain of mouse shisa 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M0W
- Type
- protein
- Length
- 63 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein shisa-3 homolog
- UniProt
- Q3UPR0
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein shisa-3 homolog | protein | 63 | 10% helix, 30% strand | Q3UPR0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide, 1 modified (disulfide, cyclization).
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 Q3UPR0
- Elsewhere: RCSB PDB 5M0W · PDBe 5M0W · UniProt Q3UPR0
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