Research workbench
Murine acyloxyacyl hydrolase (aoah), S262A mutant, with lipid a
Analyse Murine acyloxyacyl hydrolase (aoah), S262A mutant, with lipid a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W7F
- Type
- protein
- Length
- 1,050 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyloxyacyl hydrolase
- EC
- 3.1.1.77
- UniProt
- O35298
- Ligands
- FTT, DAO, NAG, GCS, CA
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyloxyacyl hydrolase (EC 3.1.1.77) | protein | 522 | 46% helix, 7% strand | O35298 |
| B | Acyloxyacyl hydrolase (EC 3.1.1.77) | protein | 528 | 45% helix, 8% strand | O35298 |
Ligands and binding sites
- FTT · 3-hydroxy-tetradecanoic acid · ligand · 2 copies · chains A, B
- DAO · Lauric acid · ligand · 2 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- GCS · 2-amino-2-deoxy-beta-D-glucopyranose · sugar · chains B
- CA · Calcium ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 812 | 0.77 | 0.80 | 79 | FTT, DAO |
| 2 | 813 | 0.77 | 0.80 | 67 | FTT, DAO |
| 3 | 61 | 0.72 | 0.98 | 18 | empty |
| 4 | 1157 | 0.71 | 0.75 | 77 | empty |
| 5 | 51 | 0.70 | 0.98 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 779 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 16 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
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 O35298
- Elsewhere: RCSB PDB 5W7F · PDBe 5W7F · UniProt O35298
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