Research workbench
Crystal structure of UPF0291 protein ynzc from bacillus subtilis at resolution 2.0 a. northeast structural genomics consortium target SR384
Analyse Crystal structure of UPF0291 protein ynzc from bacillus subtilis at resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BHP
- Type
- protein
- Length
- 154 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- UPF0291 protein ynzc
- UniProt
- O31818
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0291 protein ynzc | protein | 52 | 79% helix, 0% strand | O31818 |
| B | UPF0291 protein ynzc | protein | 48 | 77% helix, 0% strand | O31818 |
| C | UPF0291 protein ynzc | protein | 54 | 69% helix, 0% strand | O31818 |
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 | 132 | 0.77 | 0.95 | 27 | empty |
Interfaces
3 interfaces between chains.
- A–B · 757 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 705 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 670 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3BHP · Crystal structure of UPF0291 protein ynzC from Bacillus subtilis at resolution 2.0 A.… · the same entry in another collection · chain A against A, TM-score 1.00
- O31818 · AlphaFold monomer V2.0 prediction for UPF0291 protein ynzc (O31818) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 O31818
- Elsewhere: RCSB PDB 3BHP · PDBe 3BHP · UniProt O31818
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