Research workbench
Crystal structure of an ALPHA/BETA hydrolase superfamily protein from enterococcus faecalis
Analyse Crystal structure of an ALPHA/BETA hydrolase superfamily protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QRU
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q838Q5
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 272 | 38% helix, 15% strand | Q838Q5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.54 | 0.83 | 30 | PO4, EDO |
| 2 | 67 | 0.29 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2QRU · Crystal structure of an alpha/beta hydrolase superfamily protein from Enterococcus… · 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 Q838Q5
- Elsewhere: RCSB PDB 2QRU · PDBe 2QRU · UniProt Q838Q5
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