MolNFT v1 · #21393 · protein
Crystal structure of LYS49-phospholipase A2 from agkistrodon contortrix laticinctus, first fatty acid free form
1S8H · Phospholipase A2 homolog: “Crystal structure of LYS49-phospholipase A2 from agkistrodon contortrix laticinctus, first fatty acid free…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.61). MolNFT v1 #21393 on…
- PDB
- 1S8H
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase A2 homolog
- EC
- 3.1.1.4
- UniProt
- P49121
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A2 homolog (EC 3.1.1.4) | protein | 121 | 44% helix, 7% strand | P49121 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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 | 119 | 0.61 | 0.85 | 25 | SO4 |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1S8H · Crystal structure of Lys49-Phospholipase A2 from Agkistrodon contortrix laticinctus… · the same entry in another collection · chain A against A, TM-score 1.00
- P49121 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 homolog MT1 (P49121) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P49121
- Elsewhere: RCSB PDB 1S8H · PDBe 1S8H · UniProt P49121
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