Research workbench
Human acyloxyacyl hydrolase (aoah), proteolytically processed
Analyse Human acyloxyacyl hydrolase (aoah), proteolytically processed in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W78
- Type
- protein
- Length
- 524 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyloxyacyl hydrolase
- EC
- 3.1.1.77
- UniProt
- P28039
- Ligands
- MYR, PLM, DAO, NAG, CA
- Pockets
- 10 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyloxyacyl hydrolase (EC 3.1.1.77) | protein | 118 | 64% helix, 0% strand | P28039 |
| B | Acyloxyacyl hydrolase (EC 3.1.1.77) | protein | 406 | 42% helix, 10% strand | P28039 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 2 copies · chains A, B
- PLM · Palmitic acid · ligand · chains A, B
- DAO · Lauric acid · ligand · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.83 | 0.83 | 71 | MYR, PLM, DAO |
| 2 | 97 | 0.79 | 0.99 | 18 | empty |
| 3 | 59 | 0.69 | 0.96 | 18 | empty |
| 4 | 150 | 0.42 | 0.74 | 25 | empty |
| 5 | 142 | 0.42 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1732 Ų buried · 7 hydrogen bonds · protein-protein
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 P28039
- Elsewhere: RCSB PDB 5W78 · PDBe 5W78 · UniProt P28039
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