Research workbench
Crystal structure of B. licheniformis cdps yvmc-blic
Analyse Crystal structure of B. licheniformis cdps yvmc-blic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OQH
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein yvmc
- UniProt
- Q65EX3
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative uncharacterized protein yvmc | protein | 215 | 55% helix, 15% strand | Q65EX3 |
| B | Putative uncharacterized protein yvmc | protein | 225 | 52% helix, 15% strand | Q65EX3 |
Ligands and binding sites
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.76 | 0.92 | 33 | empty |
| 2 | 414 | 0.74 | 0.84 | 51 | empty |
| 3 | 247 | 0.72 | 0.87 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 695 Ų buried · 14 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 Q65EX3
- Elsewhere: RCSB PDB 3OQH · PDBe 3OQH · UniProt Q65EX3
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