Research workbench
Nf-kappab P65 subunit dimerization domain homodimer N202R mutation
Analyse Nf-kappab P65 subunit dimerization domain homodimer N202R mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MY7
- Type
- protein
- Length
- 209 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nf-kappab P65 (rela) subunit
- UniProt
- Q04207
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nf-kappab P65 (rela) subunit | protein | 107 | 3% helix, 44% strand | Q04207 |
| B | Nf-kappab P65 (rela) subunit | protein | 102 | 3% helix, 47% strand | Q04207 |
Interfaces
1 interface between chains.
- A–B · 681 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1MY7 · NF-kappaB p65 subunit dimerization domain homodimer N202R mutation · the same entry in another collection · chain A against A, TM-score 1.00
- Q04207 · AlphaFold monomer V2.0 prediction for transcription factor P65 (Q04207) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q04207
- Elsewhere: RCSB PDB 1MY7 · PDBe 1MY7 · UniProt Q04207
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