Research workbench
Crystal structure of the binding protein opuac in complex with glycine betaine
Analyse Crystal structure of the binding protein opuac in complex with glycine betaine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2B4L
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycine betaine-binding protein
- UniProt
- P46922
- Ligands
- BET
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycine betaine-binding protein | protein | 268 | 41% helix, 23% strand | P46922 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.32 | 0.76 | 19 | empty |
Compared structures
- 2B4L · Crystal structure of the binding protein OpuAC in complex with glycine betaine · the same entry in another collection · chain A against A, TM-score 1.00
- P46922 · AlphaFold monomer V2.0 prediction for glycine betaine-binding protein opuac (P46922) · a predicted model of the same protein · 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 P46922
- Elsewhere: RCSB PDB 2B4L · PDBe 2B4L · UniProt P46922
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