Research workbench
Crystal structure of catalytically-active phospholipase A2 with bound calcium
Analyse Crystal structure of catalytically-active phospholipase A2 with bound calcium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZL7
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypotensive phospholipase A2
- EC
- 3.1.1.4
- UniProt
- Q8AXY1
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypotensive phospholipase A2 (EC 3.1.1.4) | protein | 122 | 48% helix, 8% strand | Q8AXY1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1ZL7 · Crystal structure of catalytically-active phospholipase A2 with bound calcium · the same entry in another collection · chain A against A, TM-score 1.00
- Q8AXY1 · AlphaFold monomer V2.0 prediction for acidic phospholipase A2 btha-1 (Q8AXY1) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8AXY1
- Elsewhere: RCSB PDB 1ZL7 · PDBe 1ZL7 · UniProt Q8AXY1
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