Research workbench
Drosophila melanogaster krimper ETUD1 apo structure
Analyse Drosophila melanogaster krimper ETUD1 apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CFB
- Type
- protein
- Length
- 388 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FI20010P1
- UniProt
- A1ZAC4
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FI20010P1 | protein | 208 | 24% helix, 33% strand | A1ZAC4 |
| B | FI20010P1 | protein | 180 | 17% helix, 38% strand | A1ZAC4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.72 | 0.80 | 58 | empty |
| 2 | 76 | 0.40 | 0.78 | 18 | empty |
| 3 | 88 | 0.40 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1000 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7CFB · Drosophila melanogaster Krimper eTud1 apo structure · 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 A1ZAC4
- Elsewhere: RCSB PDB 7CFB · PDBe 7CFB · UniProt A1ZAC4
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