Research workbench
Crystal structure resolution of plasmodium falciparum FK506 binding domain (FKBP35) in complex with rapamycin at 1.4A resolution
Analyse Crystal structure resolution of plasmodium falciparum FK506 binding domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QT3
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FK506-binding protein (fkbp)-type peptidyl-propyl isomerase
- EC
- 5.2.1.8
- UniProt
- Q8I4V8
- Ligands
- DTV, RAP
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FK506-binding protein (fkbp)-type peptidyl-propyl isomerase (EC 5.2.1.8) | protein | 125 | 10% helix, 38% strand | Q8I4V8 |
Ligands and binding sites
- DTV · (2S,3S)-1,4-dimercaptobutane-2,3-diol · ligand · chains A
- RAP · Rapamycin immunosuppressant drug · 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 | 0.37 | 0.77 | 14 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4QT3 · Crystal structure resolution of Plasmodium falciparum FK506 binding domain (FKBP35) in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8I4V8 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP35 (Q8I4V8) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q8I4V8
- Elsewhere: RCSB PDB 4QT3 · PDBe 4QT3 · UniProt Q8I4V8
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