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Crystal Structure of UBIG/SAH complex
Analyse Crystal Structure of UBIG/SAH complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KDR
- Type
- protein
- Length
- 208 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.003
- Source
- Escherichia coli
- Molecule
- 3-demethylubiquinone-9 3-methyltransferase
- EC
- 2.1.1.64, 2.1.1.222
- UniProt
- P17993
- Ligands
- SAH
- Pockets
- 1 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.003 · 1 distinct chain · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-demethylubiquinone-9 3-methyltransferase (EC 2.1.1.64, 2.1.1.222) | protein | 208 | 39% helix, 27% strand | P17993 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · 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 | 341 | 0.78 | 0.88 | 48 | SAH |
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 P17993
- Elsewhere: RCSB PDB 4KDR · PDBe 4KDR · UniProt P17993
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