MolNFT v1 · #18417 · protein
Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate
1POE: “Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate”. X-ray diffraction, 2 ligands (GEL, CA), 2 pockets (best druggability 0.57). MolNFT v1 #18417 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1POE
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase A2
- EC
- 3.1.1.4
- UniProt
- P14555
- Ligands
- GEL, CA
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phospholipase A2 (EC 3.1.1.4) | protein | 124 | 44% helix, 6% strand | P14555 |
Ligands and binding sites
- GEL · 1-O-octyl-2-heptylphosphonyl-sn-glycero-3-phosphoethanolamine · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.57 | 0.79 | 28 | GEL |
| 2 | 208 | 0.56 | 0.79 | 30 | GEL |
Interfaces
1 interface between chains.
- A–B · 318 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide (disulfide).
Compared structures
- 1POE · Structures of free and inhibited human secretory phospholipase A2 from inflammatory… · the same entry in another collection · chain A against A, TM-score 1.00
- P14555 · AlphaFold monomer V2.0 prediction for phospholipase A2, membrane associated (P14555) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P14555
- Elsewhere: RCSB PDB 1POE · PDBe 1POE · UniProt P14555
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.