Research workbench
Crystallographic structure of FKBP12 from aedes aegypti
Analyse Crystallographic structure of FKBP12 from aedes aegypti in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UQI
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q1HR83
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbp-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 108 | 13% helix, 39% strand | Q1HR83 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.33 | 0.76 | 13 | MPO |
Compared structures
- 3UQI · Crystallographic structure of FKBP12 from Aedes aegypti · 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 Q1HR83
- Elsewhere: RCSB PDB 3UQI · PDBe 3UQI · UniProt Q1HR83
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