MolNFT v1 · #4663 · protein + DNA
Elk-1/DNA structure reveals how residues distal from DNA- binding surface affect DNA-recognition
1DUX: “Elk-1/DNA structure reveals how residues distal from DNA- binding surface affect DNA-recognition”. X-ray diffraction. MolNFT v1 #4663 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DUX
- Type
- protein + DNA
- Length
- 224 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19419
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | dna | 13 | — | — |
| B, E | — | dna | 13 | — | — |
| C, F | — | protein | 86 | — | P19419 |
Compared structures
- 1DUX · Elk-1/DNA structure reveals how residues distal from DNA-binding surface affect… · the same entry in another collection · chain F against F, TM-score 1.00
- P19419 · AlphaFold monomer V2.0 prediction for ets domain-containing protein elk-1 (P19419) · a predicted model of the same protein · chain C against A, TM-score 0.95
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 P19419
- Elsewhere: RCSB PDB 1DUX · PDBe 1DUX · UniProt P19419
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