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Crystal structure of the C-terminal domain of the hrcqb protein from pseudomonas syringae pv. phaseolicola
Analyse Crystal structure of the C-terminal domain of the hrcqb protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O9Y
- Type
- protein
- Length
- 286 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HRCQ2
- UniProt
- O85094
Structure
x-ray diffraction · 3 distinct chains · 11% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | HRCQ2 | protein | 71 | 7% helix, 62% strand | O85094 |
| C | HRCQ2 | protein | 72 | 14% helix, 61% strand | O85094 |
| D | HRCQ2 | protein | 72 | 13% helix, 61% strand | O85094 |
Interfaces
6 interfaces between chains.
- B–C · 2164 Ų buried · 39 hydrogen bonds · protein-protein
- A–D · 2118 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 481 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 226 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 87 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1O9Y · Crystal structure of the C-terminal domain of the HrcQb protein from Pseudomonas syringae… · the same entry in another collection · chain A against A, TM-score 1.00
- O85094 · AlphaFold monomer V2.0 prediction for type III secretion protein hrcqb (O85094) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O85094
- Elsewhere: RCSB PDB 1O9Y · PDBe 1O9Y · UniProt O85094
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