Research workbench
Cyclopropane fatty acid synthase from E. COLI
Analyse Cyclopropane fatty acid synthase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BQC
- Type
- protein
- Length
- 348 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclopropane-fatty-acyl-phospholipid synthase
- EC
- 2.1.1.79
- UniProt
- P0A9H8
- Ligands
- LOP, CO3
- Pockets
- 1 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclopropane-fatty-acyl-phospholipid synthase (EC 2.1.1.79) | protein | 348 | 50% helix, 18% strand | P0A9H8 |
Ligands and binding sites
- LOP · (1R)-2-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(dodecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate · ligand · chains A
- CO3 · Carbonate ion · ion · chains A
- GOL · Glycerol · additive · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.84 | 0.84 | 99 | CO3, LOP |
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 P0A9H8
- Elsewhere: RCSB PDB 6BQC · PDBe 6BQC · UniProt P0A9H8
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