Research workbench
Crystal structure of the nf-YB/NF-yc histone pair
Analyse Crystal structure of the nf-YB/NF-yc histone pair in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N1J
- Type
- protein
- Length
- 165 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nf-yb; Nf-yc
- UniProt
- P25208, Q13952
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nf-yb | protein | 87 | 72% helix, 3% strand | P25208 |
| B | Nf-yc | protein | 78 | 63% helix, 4% strand | Q13952 |
Interfaces
1 interface between chains.
- A–B · 2293 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 1N1J · Crystal structure of the NF-YB/NF-YC histone pair · the same entry in another collection · chain A against A, TM-score 1.00
- Q13952 · AlphaFold monomer V2.0 prediction for nuclear transcription factor Y subunit gamma… · a predicted model of the same protein · chain B against A, TM-score 0.94
- P25208 · AlphaFold monomer V2.0 prediction for nuclear transcription factor Y subunit beta (P25208) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P25208
- Every structure of UniProt Q13952
- Elsewhere: RCSB PDB 1N1J · PDBe 1N1J · UniProt P25208 · UniProt Q13952
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