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Crystal structure of an acid stress chaperone hdeb (KPN_03484) from klebsiella pneumoniae subsp. pneumoniae mgh 78578 at 1.70 a resolution
Analyse Crystal structure of an acid stress chaperone hdeb (KPN_03484) from klebsiella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XVV
- Type
- protein
- Length
- 150 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acid stress chaperone hdeb
- UniProt
- A6TE95
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acid stress chaperone hdeb | protein | 77 | 68% helix, 3% strand | A6TE95 |
| B | Acid stress chaperone hdeb | protein | 73 | 63% helix, 3% strand | A6TE95 |
Interfaces
1 interface between chains.
- A–B · 1161 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 4XVV · Crystal structure of an Acid stress chaperone HdeB (KPN_03484) from Klebsiella pneumoniae… · 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 A6TE95
- Elsewhere: RCSB PDB 4XVV · PDBe 4XVV · UniProt A6TE95
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