Research workbench
Combining crystallography and molecular dynamics: the case of schistosoma mansoni phospholipid glutathione peroxidase
Analyse Combining crystallography and molecular dynamics: the case of schistosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WGR
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione peroxidase
- EC
- 1.11.1.9
- UniProt
- Q00277
- Ligands
- POP
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione peroxidase (EC 1.11.1.9) | protein | 163 | 36% helix, 20% strand | Q00277 |
Ligands and binding sites
- POP · Pyrophosphate 2- · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2WGR · Combining crystallography and molecular dynamics: The case of Schistosoma mansoni… · 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 Q00277
- Elsewhere: RCSB PDB 2WGR · PDBe 2WGR · UniProt Q00277
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