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Truncated hemolysin A from P. mirabilis at 2.0 Angstroms resolution crystallized in a high salt condition
Analyse Truncated hemolysin A from P. mirabilis at 2.0 Angstroms resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KEH
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.551
- Source
- Proteus mirabilis
- Molecule
- Hemolysin
- UniProt
- P16466
Structure
x-ray diffraction · resolution 1.551 · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin | protein | 242 | 0% helix, 54% strand | P16466 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5KEH · Truncated hemolysin a from P. mirabilis at 2.0 ångströms resolution crystallized in a… · the same entry in another collection · chain A against A, TM-score 1.00
- P16466 · AlphaFold monomer V2.0 prediction for hemolysin (P16466) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P16466
- Elsewhere: RCSB PDB 5KEH · PDBe 5KEH · UniProt P16466
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