Research workbench
Crystal structure of ecarpholin S (SER49-PLA2) complexed with fatty acid
Analyse Crystal structure of ecarpholin S (SER49-PLA2) complexed with fatty acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QHD
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P48650
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 122 | — | P48650 |
Compared structures
- 2QHD · Crystal structure of ecarpholin S (ser49-PLA2) complexed with fatty acid · the same entry in another collection · chain A against A, TM-score 1.00
- P48650 · AlphaFold monomer V2.0 prediction for basic phospholipase A2 homolog ecarpholin S (P48650) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P48650
- Elsewhere: RCSB PDB 2QHD · PDBe 2QHD · UniProt P48650
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