Research workbench
Histone fold domain of atnf-YB2/NF-YC3 in I2
Analyse Histone fold domain of atnf-YB2/NF-YC3 in I2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R0N
- Type
- protein
- Length
- 171 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A178UPH7, A0A178WGU5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 91 | — | A0A178UPH7 |
| B | — | protein | 80 | — | A0A178WGU5 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6R0N · Histone fold domain of AtNF-YB2/NF-YC3 in I2 · 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 A0A178UPH7
- Every structure of UniProt A0A178WGU5
- Elsewhere: RCSB PDB 6R0N · PDBe 6R0N · UniProt A0A178UPH7 · UniProt A0A178WGU5
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