Research workbench
Misreading chaperone-substrate complexes from random noise
Analyse Misreading chaperone-substrate complexes from random noise in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BIE
- Type
- protein
- Length
- 194 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic chaperone spy
- UniProt
- P77754
- Ligands
- ZN, MG, CL
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Periplasmic chaperone spy | protein | 97 | 71% helix, 0% strand | P77754 |
Ligands and binding sites
- ZN · Zinc ion · metal · 13 copies · chains A, B
- MG · Magnesium ion · metal · chains B
- CL · Chloride ion · ion · 7 copies · chains A, B
- IMD · Imidazole · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 598 | 0.66 | 0.76 | 53 | ZN |
| 2 | 127 | 0.44 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1798 Ų buried · 26 hydrogen bonds · protein-protein
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 P77754
- Elsewhere: RCSB PDB 6BIE · PDBe 6BIE · UniProt P77754
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