MolNFT v1 · #18413 · protein
Interfacial catalysis: the mechanism of phospholipase A2
1POA: “Interfacial catalysis: the mechanism of phospholipase A2”. X-ray diffraction, 1 ligand (CA), 1 pocket (best druggability 0.56). MolNFT v1 #18413 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1POA
- Type
- protein
- Length
- 118 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase A2
- EC
- 3.1.1.4
- UniProt
- P00598
- Ligands
- CA
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A2 (EC 3.1.1.4) | protein | 118 | 47% helix, 9% strand | P00598 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 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 | 186 | 0.56 | 0.80 | 23 | empty |
Modifications
Observed in the structure: 7 disulfide (disulfide).
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 P00598
- Elsewhere: RCSB PDB 1POA · PDBe 1POA · UniProt P00598
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