Research workbench
Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex
Analyse Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F3L
- Type
- protein
- Length
- 621 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BMAL1B; Circadian locomoter output cycles protein kaput
- EC
- 2.3.1.48
- UniProt
- Q6F6D6, O08785
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | BMAL1B | protein | 302 | 37% helix, 28% strand | Q6F6D6 |
| A | Circadian locomoter output cycles protein kaput (EC 2.3.1.48) | protein | 319 | 37% helix, 28% strand | O08785 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.72 | 0.80 | 65 | empty |
| 2 | 287 | 0.70 | 0.85 | 32 | empty |
| 3 | 440 | 0.68 | 0.80 | 55 | empty |
| 4 | 400 | 0.68 | 0.80 | 31 | empty |
| 5 | 207 | 0.51 | 0.76 | 27 | empty |
Interfaces
1 interface between chains.
- B–A · 4987 Ų buried · 42 hydrogen bonds · protein-protein
Compared structures
- 4F3L · Crystal Structure of the Heterodimeric CLOCK:BMAL1 Transcriptional Activator Complex · the same entry in another collection · chain B against B, TM-score 1.00
- O08785 · AlphaFold monomer V2.0 prediction for circadian locomoter output cycles protein kaput… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q6F6D6
- Every structure of UniProt O08785
- Elsewhere: RCSB PDB 4F3L · PDBe 4F3L · UniProt Q6F6D6 · UniProt O08785
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