Research workbench
Crystal structure of histone like protein (hlp) from streptococcus mutans refined to 1.9 a resolution
Analyse Crystal structure of histone like protein (hlp) from streptococcus mutans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FBM
- Type
- protein
- Length
- 166 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein hu
- UniProt
- Q9XB21
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein hu | protein | 83 | 48% helix, 27% strand | Q9XB21 |
| B | DNA-binding protein hu | protein | 83 | 46% helix, 27% strand | Q9XB21 |
Interfaces
1 interface between chains.
- A–B · 1860 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5FBM · Crystal Structure of Histone Like Protein (HLP) from Streptococcus mutans Refined to 1.9… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9XB21 · AlphaFold monomer V2.0 prediction for DNA-binding protein hu (Q9XB21) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9XB21
- Elsewhere: RCSB PDB 5FBM · PDBe 5FBM · UniProt Q9XB21
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