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The crystal structure of prokaryotic phospholipase A2
Analyse The crystal structure of prokaryotic phospholipase A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FAZ
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospholipase A2
- EC
- 3.1.1.4
- UniProt
- Q9Z4W2
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A2 (EC 3.1.1.4) | protein | 122 | 63% helix, 0% strand | Q9Z4W2 |
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 | 110 | 0.44 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1FAZ · The crystal structure of prokaryotic phospholipase A2 · the same entry in another collection · 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 Q9Z4W2
- Elsewhere: RCSB PDB 1FAZ · PDBe 1FAZ · UniProt Q9Z4W2
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