Research workbench
Mus musculus LTC4 synthase in gsh complex form
Analyse Mus musculus LTC4 synthase in gsh complex form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NTB
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leukotriene C4 synthase
- EC
- 4.4.1.20
- UniProt
- Q60860
- Ligands
- PLM, GSH, NI, SO4
Structure
x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leukotriene C4 synthase (EC 4.4.1.20) | protein | 146 | 85% helix, 0% strand | Q60860 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 3 copies · chains A
- GSH · Glutathione · ligand · chains A
- NI · Nickel (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q60860
- Elsewhere: RCSB PDB 4NTB · PDBe 4NTB · UniProt Q60860
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