Research workbench
Complex structure of SAV1 and dendrin
Analyse Complex structure of SAV1 and dendrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BQG
- Type
- protein
- Length
- 85 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein salvador homolog 1,DENDRIN
- UniProt
- Q8VEB2, Q80TS7
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein salvador homolog 1,DENDRIN | protein | 85 | 0% helix, 33% strand | Q8VEB2, Q80TS7 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7BQG · Complex structure of SAV1 and Dendrin · the same entry in another collection · chain A against A, TM-score 1.00
- Q8VEB2 · AlphaFold monomer V2.0 prediction for protein salvador homolog 1 (Q8VEB2) · a predicted model of the same protein · chain A against A, TM-score 0.49
- Q80TS7 · AlphaFold monomer V2.0 prediction for dendrin (Q80TS7) · a predicted model of the same protein · chain A against A, TM-score 0.22
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 Q8VEB2
- Every structure of UniProt Q80TS7
- Elsewhere: RCSB PDB 7BQG · PDBe 7BQG · UniProt Q8VEB2 · UniProt Q80TS7
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