Research workbench
Crystal structure of btrn in complex with adomet and 2-doia
Analyse Crystal structure of btrn in complex with adomet and 2-doia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M7T
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Btrn
- UniProt
- Q8G907
- Ligands
- SF4, SAM, 25W
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Btrn | protein | 246 | 31% helix, 14% strand | Q8G907 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · 2 copies · chains A
- SAM · S-adenosylmethionine · ligand · chains A
- 25W · (1R,2S,3S,4R,5S)-5-aminocyclohexane-1,2,3,4-tetrol · ligand · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.85 | 0.94 | 36 | SF4, SAM, 25W |
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 Q8G907
- Elsewhere: RCSB PDB 4M7T · PDBe 4M7T · UniProt Q8G907
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