MolNFT v2 · #6075 · protein
Crystal structure of the histone from methanopyrus kandleri
1F1E · Histone fold protein: “Crystal structure of the histone from methanopyrus kandleri”. X-ray diffraction at 1.37, 1 ligand (CL). MolNFT v2 #6075 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1F1E
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.37
- Source
- Methanopyrus kandleri
- Molecule
- Histone fold protein
- UniProt
- O93641
- Ligands
- CL
Structure
x-ray diffraction · resolution 1.37 · 1 distinct chain · 66% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone fold protein | protein | 151 | 66% helix, 5% strand | O93641 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 1F1E · Crystal structure of the histone from methanopyrus kandleri · 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 O93641
- Elsewhere: RCSB PDB 1F1E · PDBe 1F1E · UniProt O93641
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