MolNFT v1 · #126320 · protein
Fragment-based inhibitors of lipoprotein associated phospholipase A2
5LZ5: “Fragment-based inhibitors of lipoprotein associated phospholipase A2”. X-ray diffraction, 2 ligands (7K4, CL). MolNFT v1 #126320 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5LZ5
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13093
- Ligands
- 7K4, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 371 | — | Q13093 |
Ligands and binding sites
- 7K4 · 2-fluoranyl-5-[2-[(4~{S})-4-methyl-2-oxidanylidene-4-phenyl-pyrrolidin-1-yl]ethoxy]benzenecarbonitrile · ligand · chains A
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LZ5 · Fragment-based inhibitors of Lipoprotein associated Phospholipase A2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q13093 · AlphaFold monomer V2.0 prediction for platelet-activating factor acetylhydrolase (Q13093) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q13093
- Elsewhere: RCSB PDB 5LZ5 · PDBe 5LZ5 · UniProt Q13093
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