Research workbench
Solution NMR structure of the DNA-binding domain of human nf-E2- related factor 2, northeast structural genomics consortium (nesg) target HR3520O
Analyse Solution NMR structure of the DNA-binding domain of human nf-E2- related factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LZ1
- Type
- protein
- Length
- 90 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16236
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 90 | — | Q16236 |
Compared structures
- 2LZ1 · Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2… · the same entry in another collection · chain A against A, TM-score 1.00
- Q16236 · AlphaFold monomer V2.0 prediction for nuclear factor erythroid 2-related factor 2 (Q16236) · a predicted model of the same protein · chain A against A, TM-score 0.54
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 Q16236
- Elsewhere: RCSB PDB 2LZ1 · PDBe 2LZ1 · UniProt Q16236
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