Research workbench
The crystal structure of cyclopropane-fatty-acyl-phospholipid synthase from lactobacillus acidophilus
Analyse The crystal structure of cyclopropane-fatty-acyl-phospholipid synthase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Z9O
- Type
- protein
- Length
- 745 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclopropane-fatty-acyl-phospholipid synthase
- EC
- 2.1.1.79
- UniProt
- Q5FJM0
- Ligands
- EPH, CO3
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) | protein | 373 | 43% helix, 19% strand | Q5FJM0 |
| B | Cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) | protein | 372 | 42% helix, 19% strand | Q5FJM0 |
Ligands and binding sites
- EPH · L-alpha-phosphatidyl-beta-oleoyl-gamma-palmitoyl-phosphatidylethanolamine · ligand · 2 copies · chains A, B
- CO3 · Carbonate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.84 | 0.85 | 101 | CO3, EPH |
| 2 | 925 | 0.84 | 0.85 | 95 | CO3, EPH |
| 3 | 123 | 0.47 | 0.79 | 24 | empty |
| 4 | 144 | 0.41 | 0.74 | 23 | empty |
| 5 | 67 | 0.29 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 396 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5Z9O · The crystal structure of Cyclopropane-fatty-acyl-phospholipid synthase from Lactobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5FJM0
- Elsewhere: RCSB PDB 5Z9O · PDBe 5Z9O · UniProt Q5FJM0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.