MolNFT v1 · #80821 · protein
Functionally selective inhibition of group iia phospholipase A2 reveals a role for vimentin in regulating arachidonic acid metabolism
3U8I · Phospholipase A2, membrane associated: “Functionally selective inhibition of group iia phospholipase A2 reveals a role for vimentin in regulating…”. X-ray diffraction, 3 ligands (CA, NA, CL), 2 pockets (best druggability 0.72).…
- PDB
- 3U8I
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase A2, membrane associated
- EC
- 3.1.1.4
- UniProt
- P14555
- Ligands
- CA, NA, CL
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phospholipase A2, membrane associated (EC 3.1.1.4) | protein | 124 | 50% helix, 6% strand | P14555 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
- NA · Sodium ion · metal · 4 copies · chains A, B
- CL · Chloride ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.72 | 0.80 | 61 | empty |
| 2 | 141 | 0.46 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 605 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 3U8I · Functionally selective inhibition of Group IIA phospholipase A2 reveals a role for… · 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 0.97
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 3U8I · PDBe 3U8I · UniProt P14555
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