Research workbench
X-ray crystal structure of protein BH3568 from bacillus halodurans. northeast structural genomics consortium BHR60.
Analyse X-ray crystal structure of protein BH3568 from bacillus halodurans. northeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HZB
- Type
- protein
- Length
- 1,244 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical UPF0052 protein BH3568
- UniProt
- Q9K706
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Hypothetical UPF0052 protein BH3568 | protein | 311 | 40% helix, 19% strand | Q9K706 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.71 | 0.87 | 23 | empty |
| 2 | 192 | 0.70 | 0.87 | 23 | empty |
| 3 | 343 | 0.59 | 0.77 | 46 | empty |
| 4 | 352 | 0.59 | 0.77 | 45 | empty |
| 5 | 302 | 0.59 | 0.78 | 41 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1106 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 1092 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified, 4 disulfide (engineered, disulfide).
Compared structures
- 2HZB · X-Ray Crystal Structure of Protein BH3568 from Bacillus halodurans. Northeast Structural… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9K706 · AlphaFold monomer V2.0 prediction for gluconeogenesis factor (Q9K706) · 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 Q9K706
- Elsewhere: RCSB PDB 2HZB · PDBe 2HZB · UniProt Q9K706
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