Research workbench
The crystal structure of a functionally unknown protein from listeria monocytogenes egd-E
Analyse The crystal structure of a functionally unknown protein from listeria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EAE
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LMO1068 protein
- UniProt
- Q8Y850
- Ligands
- MLT, NA
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LMO1068 protein | protein | 184 | 16% helix, 38% strand | Q8Y850 |
| B | LMO1068 protein | protein | 188 | 16% helix, 38% strand | Q8Y850 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 465 | 0.70 | 0.81 | 69 | MLT |
Interfaces
1 interface between chains.
- A–B · 819 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4EAE · The crystal structure of a functionally unknown protein from Listeria monocytogenes EGD-e · 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 Q8Y850
- Elsewhere: RCSB PDB 4EAE · PDBe 4EAE · UniProt Q8Y850
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