Research workbench
Crystal structure of BetP with asymmetric protomers.
Analyse Crystal structure of BetP with asymmetric protomers. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AIN
- Type
- protein
- Length
- 1,525 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.1
- Source
- CORYNEBACTERIUM GLUTAMICUM
- Molecule
- Glycine betaine transporter betp
- UniProt
- P54582
- Ligands
- BET, CM5, NA, CL
- Pockets
- 19 · best druggability 0.77
Structure
x-ray diffraction · resolution 3.1 · 3 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycine betaine transporter betp | protein | 529 | 75% helix, 0% strand | P54582 |
| B | Glycine betaine transporter betp | protein | 497 | 78% helix, 0% strand | P54582 |
| C | Glycine betaine transporter betp | protein | 499 | 76% helix, 0% strand | P54582 |
Ligands and binding sites
- BET · Trimethyl glycine · ligand · 2 copies · chains B, C
- CM5 · 5-cyclohexyl-1-pentyl-beta-D-maltoside · ligand · chains C
- NA · Sodium ion · metal · chains B
- CL · Chloride ion · ion · 4 copies · chains A, B, C
- PEG · Di(hydroxyethyl)ether · additive · chains B
- FLC · Citrate anion · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.77 | 0.87 | 48 | BET |
| 2 | 976 | 0.76 | 0.78 | 105 | CL |
| 3 | 194 | 0.54 | 0.79 | 33 | empty |
| 4 | 208 | 0.50 | 0.76 | 24 | CL |
| 5 | 150 | 0.49 | 0.77 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1022 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 742 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 719 Ų buried · 7 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 P54582
- Elsewhere: RCSB PDB 4AIN · PDBe 4AIN · UniProt P54582
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