MolNFT v1 · #5242 · protein
Ovine pghs-1 complexed with salicyl hydroxamic acid
1EBV · Prostaglandin H2 synthase: “Ovine pghs-1 complexed with salicyl hydroxamic acid”. X-ray diffraction, 3 ligands (SCL, HEM, NAG), 4 pockets (best druggability 0.79). MolNFT v1 #5242 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1EBV
- Type
- protein
- Length
- 551 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostaglandin H2 synthase
- EC
- 1.14.99.1
- UniProt
- P05979
- Ligands
- SCL, HEM, NAG
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostaglandin H2 synthase (EC 1.14.99.1) | protein | 551 | 46% helix, 10% strand | P05979 |
Ligands and binding sites
- SCL · Acetic acid salicyloyl-amino-ester · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 952 | 0.79 | 0.81 | 86 | SCL |
| 2 | 440 | 0.67 | 0.79 | 38 | HEM |
| 3 | 108 | 0.35 | 0.73 | 21 | empty |
| 4 | 55 | 0.27 | 0.74 | 17 | empty |
Modifications
Observed in the structure: 5 disulfide, 3 glycan, 1 modified (disulfide, N-glycosylation, nonstandard).
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 P05979
- Elsewhere: RCSB PDB 1EBV · PDBe 1EBV · UniProt P05979
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