Research workbench
Discovery of a potent cyclophilin inhibitor (compound 5) based on structural simplification of sanglifehrin a
Analyse Discovery of a potent cyclophilin inhibitor (compound 5) based on structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T9W
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a
- EC
- 5.2.1.8
- UniProt
- P62937
- Ligands
- 78E
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase a (EC 5.2.1.8) | protein | 164 | 15% helix, 32% strand | P62937 |
Ligands and binding sites
- 78E · 3-[(3-hydroxyphenyl)methyl]-6-(propan-2-yl)-19-oxa-1,4, 7,25-tetraazabicyclo[19.3.1]pentacosa-13,15-diene-2,5, 8,20-tetrone · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5T9W · Discovery of a Potent Cyclophilin Inhibitor (Compound 5) based on Structural… · 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 P62937
- Elsewhere: RCSB PDB 5T9W · PDBe 5T9W · UniProt P62937
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