Research workbench
Crystal structure of plant phospholipase D alpha
Analyse Crystal structure of plant phospholipase D alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KZ9
- Type
- protein
- Length
- 770 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase D alpha 1
- EC
- 3.1.4.4
- UniProt
- Q38882
- Ligands
- CA
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase D alpha 1 (EC 3.1.4.4) | protein | 770 | 25% helix, 27% strand | Q38882 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.75 | 0.98 | 24 | empty |
| 2 | 386 | 0.74 | 0.85 | 43 | empty |
| 3 | 111 | 0.50 | 0.81 | 21 | empty |
| 4 | 163 | 0.47 | 0.77 | 30 | empty |
| 5 | 146 | 0.44 | 0.75 | 29 | empty |
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 Q38882
- Elsewhere: RCSB PDB 6KZ9 · PDBe 6KZ9 · UniProt Q38882
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.