Research workbench
Intermolecular recognition revealed by the complex structure of human clock-BMAL1 basic helix-loop-helix domains with E-box DNA
Analyse Intermolecular recognition revealed by the complex structure of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H10
- Type
- protein + DNA
- Length
- 153 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O00327, O15516
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 60 | — | O00327 |
| B | — | protein | 63 | — | O15516 |
| C | — | dna | 15 | — | — |
| D | — | dna | 15 | — | — |
Compared structures
- 4H10 · Intermolecular recognition revealed by the complex structure of human CLOCK-BMAL1 basic… · the same entry in another collection · chain A against A, TM-score 1.00
- O00327 · AlphaFold monomer V2.0 prediction for aryl hydrocarbon receptor nuclear translocator-like… · a predicted model of the same protein · chain A against A, TM-score 0.89
- O15516 · AlphaFold monomer V2.0 prediction for circadian locomoter output cycles protein kaput… · a predicted model of the same protein · chain B against A, TM-score 0.87
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 O00327
- Every structure of UniProt O15516
- Elsewhere: RCSB PDB 4H10 · PDBe 4H10 · UniProt O00327 · UniProt O15516
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