Research workbench
Group deposition of library data - crystal structure of ecdsba after initial refinement with no ligand modelled (structure B1_1)
Analyse Group deposition of library data - crystal structure of ecdsba after initial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QKU
- Type
- protein
- Length
- 376 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- THIOL:DISULFIDE interchange protein
- UniProt
- A0A073FPA6
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | THIOL:DISULFIDE interchange protein | protein | 188 | 54% helix, 11% strand | A0A073FPA6 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.57 | 0.77 | 37 | empty |
| 2 | 195 | 0.56 | 0.80 | 30 | empty |
| 3 | 144 | 0.49 | 0.78 | 24 | empty |
| 4 | 128 | 0.39 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 808 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 A0A073FPA6
- Elsewhere: RCSB PDB 5QKU · PDBe 5QKU · UniProt A0A073FPA6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.