Research workbench
The crystal structure of fis mutant K36E reveals that the transactivation region of the fis protein contains extended mobile beta-hairpin arms
Analyse The crystal structure of fis mutant K36E reveals that the transactivation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F36
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fis
- UniProt
- P0A6R3
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fis | protein | 89 | 58% helix, 11% strand | P0A6R3 |
Interfaces
1 interface between chains.
- A–B · 2236 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1F36 · The crystal structure of fis mutant K36E reveals that the transactivation region of the… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6R3 · AlphaFold monomer V2.0 prediction for DNA-binding protein fis (P0A6R3) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P0A6R3
- Elsewhere: RCSB PDB 1F36 · PDBe 1F36 · UniProt P0A6R3
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