MolNFT v1 · #70057 · protein
Structure of pvdq covalently acylated with myristate
3L94 · Acyl-homoserine lactone acylase pvdq subunit alpha: “Structure of pvdq covalently acylated with myristate”. X-ray diffraction, 1 ligand (MYR), 8 pockets (best druggability 0.73). MolNFT v1 #70057 on GenesisL1: 3D structure, binding…
- PDB
- 3L94
- Type
- protein
- Length
- 707 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-homoserine lactone acylase pvdq subunit alpha; Acyl-homoserine lactone acylase pvdq…
- EC
- 3.5.1.97
- UniProt
- Q9I194
- Ligands
- MYR
- Pockets
- 8 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-homoserine lactone acylase pvdq subunit alpha (EC 3.5.1.97) | protein | 163 | 61% helix, 9% strand | Q9I194 |
| B | Acyl-homoserine lactone acylase pvdq subunit beta (EC 3.5.1.97) | protein | 544 | 26% helix, 32% strand | Q9I194 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 650 | 0.73 | 0.80 | 85 | EDO, MYR |
| 2 | 150 | 0.45 | 0.76 | 25 | EDO |
| 3 | 176 | 0.44 | 0.74 | 33 | empty |
| 4 | 50 | 0.39 | 0.82 | 17 | EDO |
| 5 | 62 | 0.39 | 0.80 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3961 Ų buried · 54 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide, 1 lipid (disulfide, myristoylation).
Compared structures
- 3L94 · Structure of PvdQ covalently acylated with myristate · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I194 · AlphaFold monomer V2.0 prediction for acyl-homoserine lactone acylase pvdq (Q9I194) · 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 Q9I194
- Elsewhere: RCSB PDB 3L94 · PDBe 3L94 · UniProt Q9I194
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