MolNFT v1 · #165991 · protein
Transcription factor deltafosb bzip domain self-assembly, type-II crystal
6UCM · Protein fosb: “Transcription factor deltafosb bzip domain self-assembly, type-II crystal”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.35). MolNFT v1 #165991 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6UCM
- Type
- protein
- Length
- 154 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein fosb
- UniProt
- P53539
- Ligands
- CA
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 3 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fosb | protein | 39 | 92% helix, 0% strand | P53539 |
| B | Protein fosb | protein | 50 | 96% helix, 0% strand | P53539 |
| C | Protein fosb | protein | 65 | 97% helix, 0% strand | P53539 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.35 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1052 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 512 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 335 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P53539
- Elsewhere: RCSB PDB 6UCM · PDBe 6UCM · UniProt P53539
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