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Crystal structure of human ps-1
Analyse Crystal structure of human ps-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AL0
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostaglandin E synthase
- EC
- 5.3.99.3
- UniProt
- O14684
- Ligands
- PLM, GSH
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin E synthase (EC 5.3.99.3) | protein | 146 | 79% helix, 1% strand | O14684 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 3 copies · chains A
- GSH · Glutathione · ligand · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 2 copies · 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 O14684
- Elsewhere: RCSB PDB 4AL0 · PDBe 4AL0 · UniProt O14684
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