Research workbench
Structure-function analysis of human L-prostaglandin D synthase bound with fatty acid
Analyse Structure-function analysis of human L-prostaglandin D synthase bound with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3O22
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostaglandin-H2 D-isomerase
- EC
- 5.3.99.2
- UniProt
- P41222
- Ligands
- OLA, PLM
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin-H2 D-isomerase (EC 5.3.99.2) | protein | 157 | 20% helix, 47% strand | P41222 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 319 | 0.70 | 0.83 | 28 | OLA, PLM |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3O22 · Structure-function analysis of human L-Prostaglandin D Synthase bound with fatty acid · the same entry in another collection · chain A against A, TM-score 1.00
- P41222 · AlphaFold monomer V2.0 prediction for prostaglandin-H2 D-isomerase (P41222) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P41222
- Elsewhere: RCSB PDB 3O22 · PDBe 3O22 · UniProt P41222
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