Research workbench
The crystal structure of a conserved protein of unknown function from streptococcus thermophilus lmg 18311.
Analyse The crystal structure of a conserved protein of unknown function from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QZI
- Type
- protein
- Length
- 401 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q5M594
- Ligands
- NA
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Uncharacterized protein | protein | 101 | 30% helix, 39% strand | Q5M594 |
| D | Uncharacterized protein | protein | 98 | 18% helix, 37% strand | Q5M594 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.61 | 0.78 | 39 | empty |
| 2 | 330 | 0.61 | 0.78 | 46 | empty |
| 3 | 236 | 0.51 | 0.76 | 39 | empty |
| 4 | 52 | 0.45 | 0.85 | 16 | empty |
| 5 | 110 | 0.42 | 0.77 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–D · 591 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 559 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 407 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 339 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 43 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 2QZI · The crystal structure of a conserved protein of unknown function from Streptococcus… · 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 Q5M594
- Elsewhere: RCSB PDB 2QZI · PDBe 2QZI · UniProt Q5M594
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