Research workbench
Crystal structure of the histone hmfa from methanothermus fervidus
Analyse Crystal structure of the histone hmfa from methanothermus fervidus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HTA
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone hmfa
- UniProt
- P48781
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone hmfa | protein | 68 | 69% helix, 0% strand | P48781 |
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.
Compared structures
- 1HTA · Crystal structure of the histone hmfa from methanothermus fervidus · the same entry in another collection · chain A against A, TM-score 1.00
- P48781 · AlphaFold monomer V2.0 prediction for DNA-binding protein hmf-1 (P48781) · a predicted model of the same protein · chain A 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 P48781
- Elsewhere: RCSB PDB 1HTA · PDBe 1HTA · UniProt P48781
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