Research workbench
Crystal structure of cait R262E bound to gamma-butyrobetaine
Analyse Crystal structure of cait R262E bound to gamma-butyrobetaine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M8J
- Type
- protein
- Length
- 495 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-CARNITINE/GAMMA-butyrobetaine antiporter
- UniProt
- C2LLR0
- Ligands
- NM2
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-CARNITINE/GAMMA-butyrobetaine antiporter | protein | 495 | 79% helix, 1% strand | C2LLR0 |
Ligands and binding sites
- NM2 · 3-carboxy-N,N,N-trimethylpropan-1-aminium · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1033 | 0.81 | 0.82 | 72 | NM2 |
| 2 | 218 | 0.59 | 0.80 | 25 | empty |
| 3 | 98 | 0.46 | 0.80 | 20 | empty |
| 4 | 55 | 0.25 | 0.72 | 15 | empty |
Compared structures
- 4M8J · Crystal structure of CaiT R262E bound to gamma-butyrobetaine · the same entry in another collection · 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 C2LLR0
- Elsewhere: RCSB PDB 4M8J · PDBe 4M8J · UniProt C2LLR0
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