Research workbench
Cyclophilin A complexed with tri-vector ligand 10.
Analyse Cyclophilin A complexed with tri-vector ligand 10. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GJL
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.16
- Source
- Homo sapiens
- Molecule
- Peptidyl-prolyl cis-trans isomerase A
- EC
- 5.2.1.8
- UniProt
- P62937
- Ligands
- F1Q
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · resolution 1.16 · 1 distinct chain · 14% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase A (EC 5.2.1.8) | protein | 165 | 14% helix, 33% strand | P62937 |
Ligands and binding sites
- F1Q · ethyl 2-[[(4-aminophenyl)methyl-(1~{H}-1,2,3,4-tetrazol-5-ylmethyl)carbamoyl]amino]ethanoate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.33 | 0.77 | 16 | F1Q |
Compared structures
- 6GJL · Cyclophilin a complexed with tri-vector ligand 10. · 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 6GJL · PDBe 6GJL · UniProt P62937
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