Research workbench
Crystal structure of the yersinia secretion chaperone syce
Analyse Crystal structure of the yersinia secretion chaperone syce in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K6Z
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type III secretion chaperone syce
- UniProt
- P31491
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type III secretion chaperone syce | protein | 122 | 30% helix, 30% strand | P31491 |
| B | Type III secretion chaperone syce | protein | 121 | 31% helix, 30% strand | P31491 |
Ligands and binding sites
- IMD · Imidazole · additive · 2 copies · chains A, B
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 | 260 | 0.75 | 0.89 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 1409 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
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 P31491
- Elsewhere: RCSB PDB 1K6Z · PDBe 1K6Z · UniProt P31491
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.