Research workbench
Crystal structure of the factor for inversion stimulation fis at 2.0 ångströms resolution
Analyse Crystal structure of the factor for inversion stimulation fis at 2.0 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FIA
- Type
- protein
- Length
- 157 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Factor for inversion stimulation (fis)
- UniProt
- P0A6R3
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Factor for inversion stimulation (fis) | protein | 79 | 66% helix, 3% strand | P0A6R3 |
| B | Factor for inversion stimulation (fis) | protein | 78 | 67% helix, 3% strand | P0A6R3 |
Interfaces
1 interface between chains.
- A–B · 2035 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 1FIA · Crystal structure of the factor for inversion stimulation fis at 2.0 ångströms resolution · 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 B 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 P0A6R3
- Elsewhere: RCSB PDB 1FIA · PDBe 1FIA · UniProt P0A6R3
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