Research workbench
Crystal structure of full-length benm
Analyse Crystal structure of full-length benm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K1N
- Type
- protein
- Length
- 608 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator benm
- UniProt
- O68014
- Ligands
- CL
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional regulator benm | protein | 303 | 45% helix, 20% strand | O68014 |
| B | Hth-type transcriptional regulator benm | protein | 305 | 44% helix, 21% strand | O68014 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.61 | 0.81 | 30 | empty |
| 2 | 150 | 0.55 | 0.81 | 26 | empty |
| 3 | 118 | 0.55 | 0.83 | 23 | empty |
| 4 | 61 | 0.43 | 0.82 | 17 | empty |
| 5 | 162 | 0.42 | 0.74 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 956 Ų buried · 20 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 O68014
- Elsewhere: RCSB PDB 3K1N · PDBe 3K1N · UniProt O68014
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