Research workbench
High resolution structure of the asymmetric R333G hamp-dhp mutant
Analyse High resolution structure of the asymmetric R333G hamp-dhp mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZCC
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hamp, osmolarity sensor protein envz
- EC
- 2.7.13.3
- UniProt
- O28769, P0AEJ4
Structure
x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hamp, osmolarity sensor protein envz (EC 2.7.13.3) | protein | 110 | 80% helix, 0% strand | O28769, P0AEJ4 |
Interfaces
1 interface between chains.
- A–B · 2345 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3ZCC · High resolution structure of the asymmetric R333G Hamp-Dhp mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P0AEJ4 · AlphaFold monomer V2.0 prediction for sensor histidine kinase envz (P0AEJ4) · a predicted model of the same protein · chain B against A, TM-score 0.69
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 O28769
- Every structure of UniProt P0AEJ4
- Elsewhere: RCSB PDB 3ZCC · PDBe 3ZCC · UniProt O28769 · UniProt P0AEJ4
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