Research workbench
C-terminal condensation domain of ebony in complex with carcinine
Analyse C-terminal condensation domain of ebony in complex with carcinine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DYR
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ebony
- UniProt
- A4GK78
- Ligands
- HJD
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ebony | protein | 213 | 41% helix, 23% strand | A4GK78 |
Ligands and binding sites
- HJD · N-[2-(1H-imidazol-5-yl)ethyl]-beta-alaninamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.76 | 0.85 | 56 | HJD |
Compared structures
- 6DYR · C-terminal condensation domain of Ebony in complex with Carcinine · the same entry in another collection · chain A against A, TM-score 1.00
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 A4GK78
- Elsewhere: RCSB PDB 6DYR · PDBe 6DYR · UniProt A4GK78
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