Research workbench
Structure of the C-terminal domain of EHD1 with fnyestnpftak
Analyse Structure of the C-terminal domain of EHD1 with fnyestnpftak in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KFF
- Type
- protein
- Length
- 117 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eh domain-containing protein 1; RAB11-FIP2 npf peptide fnyestnpftak
- UniProt
- Q9H4M9
- Ligands
- CA
Structure
solution nmr · 2 distinct chains · 44% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eh domain-containing protein 1 | protein | 105 | 50% helix, 5% strand | Q9H4M9 |
| B | RAB11-FIP2 npf peptide fnyestnpftak | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 299 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2KFF · Structure of the C-terminal domain of EHD1 with FNYESTNPFTAK · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H4M9 · AlphaFold monomer V2.0 prediction for eh domain-containing protein 1 (Q9H4M9) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q9H4M9
- Elsewhere: RCSB PDB 2KFF · PDBe 2KFF · UniProt Q9H4M9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.