Research workbench
Structure of an asfv-derived histone-like protein PA104R
Analyse Structure of an asfv-derived histone-like protein PA104R in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LMH
- Type
- protein
- Length
- 198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PA104R
- UniProt
- A0A0A1E0L7
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | PA104R | protein | 99 | 39% helix, 30% strand | A0A0A1E0L7 |
Interfaces
1 interface between chains.
- A–B · 2441 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6LMH · Structure of an ASFV-derived histone-like protein pA104R · 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 A0A0A1E0L7
- Elsewhere: RCSB PDB 6LMH · PDBe 6LMH · UniProt A0A0A1E0L7
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