Research workbench
Crystal structure of a putative transcriptional regulator from saccharomonospora viridis in complex with N,N-dimethylmethanamine
Analyse Crystal structure of a putative transcriptional regulator from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NEL
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator
- UniProt
- C7MT25
- Ligands
- KEN
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator | protein | 190 | 79% helix, 1% strand | C7MT25 |
Ligands and binding sites
- KEN · N,N-dimethylmethanamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.75 | 0.95 | 21 | KEN |
Modifications
Observed in the structure: 3 modified (engineered, artifact).
Compared structures
- 4NEL · Crystal structure of a putative transcriptional regulator from Saccharomonospora viridis… · the same entry in another collection · chain A against A, TM-score 1.00
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 C7MT25
- Elsewhere: RCSB PDB 4NEL · PDBe 4NEL · UniProt C7MT25
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