Research workbench
Crystal structure of the debrominase BMP8 (apo)
Analyse Crystal structure of the debrominase BMP8 (apo) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OHI
- Type
- protein
- Length
- 373 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Debrominase BMP8
- UniProt
- F2K073
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Debrominase BMP8 | protein | 187 | 71% helix, 0% strand | F2K073 |
| B | Debrominase BMP8 | protein | 186 | 72% helix, 0% strand | F2K073 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.57 | 0.80 | 45 | empty |
| 2 | 68 | 0.34 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2101 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6OHI · Crystal Structure of the Debrominase Bmp8 (Apo) · 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 F2K073
- Elsewhere: RCSB PDB 6OHI · PDBe 6OHI · UniProt F2K073
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