Research workbench
Murine acyloxyacyl hydrolase (aoah), S262A mutant
Analyse Murine acyloxyacyl hydrolase (aoah), S262A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W7D
- Type
- protein
- Length
- 528 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyloxyacyl hydrolase
- EC
- 3.1.1.77
- UniProt
- O35298
- Ligands
- PX8, MYR, NAG, CA
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyloxyacyl hydrolase (EC 3.1.1.77) | protein | 528 | 47% helix, 8% strand | O35298 |
Ligands and binding sites
- PX8 · 1,2-distearoyl-sn-glycero-3-phosphate · ligand · chains A
- MYR · Myristic acid · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- CA · Calcium ion · metal · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1065 | 0.82 | 0.82 | 82 | PX8, MYR |
| 2 | 64 | 0.73 | 0.98 | 20 | empty |
| 3 | 53 | 0.38 | 0.81 | 13 | empty |
| 4 | 92 | 0.36 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 8 disulfide, 3 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 5W7D · PDBe 5W7D · UniProt O35298
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