Research workbench
Crystal structure of a mutated opubc in complex with choline
Analyse Crystal structure of a mutated opubc in complex with choline in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EYQ
- Type
- protein
- Length
- 536 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Choline-binding protein
- UniProt
- Q45462
- Ligands
- CHT
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Choline-binding protein | protein | 271 | 46% helix, 20% strand | Q45462 |
| B | Choline-binding protein | protein | 265 | 46% helix, 20% strand | Q45462 |
Ligands and binding sites
- CHT · Choline ion · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.74 | 0.78 | 101 | CHT |
| 2 | 212 | 0.66 | 0.84 | 33 | CHT |
| 3 | 79 | 0.47 | 0.82 | 20 | empty |
| 4 | 112 | 0.38 | 0.74 | 20 | empty |
| 5 | 101 | 0.36 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 502 Ų buried · 9 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 Q45462
- Elsewhere: RCSB PDB 6EYQ · PDBe 6EYQ · UniProt Q45462
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