MolNFT v1 · #146953 · protein
Murine N-acylethanolamine-hydrolyzing acid amidase (naaa)
6DXY · N-acylethanolamine-hydrolyzing acid amidase subunit alpha: “Murine N-acylethanolamine-hydrolyzing acid amidase (naaa)”. X-ray diffraction, 2 ligands (NAG, CL), 3 pockets (best druggability 0.40). MolNFT v1 #146953 on GenesisL1: 3D…
- PDB
- 6DXY
- Type
- protein
- Length
- 650 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing…
- EC
- 3.5.1.60
- UniProt
- Q9D7V9
- Ligands
- NAG, CL
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | N-acylethanolamine-hydrolyzing acid amidase subunit alpha (EC 3.5.1.60) | protein | 95 | 61% helix, 5% strand | Q9D7V9 |
| B, D | N-acylethanolamine-hydrolyzing acid amidase subunit beta (EC 3.5.1.60) | protein | 230 | 28% helix, 34% strand | Q9D7V9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B, D
- CL · Chloride ion · ion · 11 copies · chains A, B, C, D
- PG4 · Tetraethylene glycol · additive · 2 copies · chains B, D
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.40 | 0.76 | 14 | empty |
| 2 | 75 | 0.33 | 0.75 | 16 | empty |
| 3 | 56 | 0.27 | 0.73 | 15 | empty |
Interfaces
5 interfaces between chains.
- A–B · 2198 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 2181 Ų buried · 28 hydrogen bonds · protein-protein
- A–D · 345 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 319 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 198 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 glycan, 2 modified (N-glycosylation, oxidation).
Compared structures
- 6DXY · Murine N-acylethanolamine-hydrolyzing acid amidase (NAAA) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9D7V9 · AlphaFold monomer V2.0 prediction for N-acylethanolamine-hydrolyzing acid amidase (Q9D7V9) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9D7V9
- Elsewhere: RCSB PDB 6DXY · PDBe 6DXY · UniProt Q9D7V9
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