MolNFT v1 · #154920 · protein
Crystal structure of phospholipase A2
6KQU · Group iie secretory phospholipase A2: “Crystal structure of phospholipase A2”. X-ray diffraction, 3 ligands (NA, CA, CL), 1 pocket (best druggability 0.48). MolNFT v1 #154920 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6KQU
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Group iie secretory phospholipase A2
- EC
- 3.1.1.4
- UniProt
- Q9NZK7
- Ligands
- NA, CA, CL
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Group iie secretory phospholipase A2 (EC 3.1.1.4) | protein | 121 | 50% helix, 8% strand | Q9NZK7 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 6 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.48 | 0.75 | 28 | 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 Q9NZK7
- Elsewhere: RCSB PDB 6KQU · PDBe 6KQU · UniProt Q9NZK7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.