Research workbench
Crystal structure of the yersinia pestis type III secretion chaperone sych in complex with a stable fragment of YSCM2
Analyse Crystal structure of the yersinia pestis type III secretion chaperone sych in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TTW
- Type
- protein
- Length
- 138 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Secretion chaperone; YSCM2
- UniProt
- Q7ARG9
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secretion chaperone | protein | 118 | 28% helix, 30% strand | Q7ARG9 |
| B | YSCM2 | protein | 20 | 40% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 660 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1TTW · Crystal structure of the Yersinia Pestis type III secretion chaperone SycH in complex… · 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 Q7ARG9
- Elsewhere: RCSB PDB 1TTW · PDBe 1TTW · UniProt Q7ARG9
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