Research workbench
X-ray structure of FIP200 claw domain
Analyse X-ray structure of FIP200 claw domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DCE
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.56
- Source
- Homo sapiens
- Molecule
- RB1-inducible coiled-coil protein 1
- UniProt
- Q8TDY2
- Ligands
- SO4
Structure
x-ray diffraction · resolution 1.56 · 1 distinct chain · 7% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RB1-inducible coiled-coil protein 1 | protein | 92 | 7% helix, 40% strand | Q8TDY2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (engineered).
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 Q8TDY2
- Elsewhere: RCSB PDB 6DCE · PDBe 6DCE · UniProt Q8TDY2
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