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The crystal structure of functionally unknown conserved protein domain from neisseria meningitidis MC58
Analyse The crystal structure of functionally unknown conserved protein domain from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OI8
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q9K0P8
- Ligands
- ADN
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 156 | 46% helix, 21% strand | Q9K0P8 |
| B | Uncharacterized protein | protein | 154 | 47% helix, 21% strand | Q9K0P8 |
Ligands and binding sites
- ADN · Adenosine · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.70 | 0.80 | 56 | ADN |
| 2 | 80 | 0.50 | 0.84 | 17 | empty |
| 3 | 51 | 0.34 | 0.78 | 8 | empty |
Interfaces
1 interface between chains.
- A–B · 2130 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3OI8 · The crystal structure of functionally unknown conserved protein domain from Neisseria… · 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 Q9K0P8
- Elsewhere: RCSB PDB 3OI8 · PDBe 3OI8 · UniProt Q9K0P8
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