Research workbench
Peptidoglycan O-acetylesterase in action, 0 min
Analyse Peptidoglycan O-acetylesterase in action, 0 min in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K40
- Type
- protein
- Length
- 698 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gdsl-like LIPASE/ACYLHYDROLASE family protein
- UniProt
- A0A0A8F713
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Gdsl-like LIPASE/ACYLHYDROLASE family protein | protein | 349 | 31% helix, 29% strand | A0A0A8F713 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1134 | 0.74 | 0.77 | 94 | empty |
| 2 | 72 | 0.44 | 0.82 | 19 | empty |
| 3 | 55 | 0.36 | 0.80 | 16 | empty |
| 4 | 58 | 0.35 | 0.78 | 17 | empty |
| 5 | 55 | 0.34 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 645 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4K40 · Peptidoglycan O-acetylesterase in action, 0 min · 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 A0A0A8F713
- Elsewhere: RCSB PDB 4K40 · PDBe 4K40 · UniProt A0A0A8F713
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