MolNFT v1 · #105047 · protein
Crystal structure resolution of plasmodium falciparum FK506 binding domain (FKBP35) in complex with rapamycin at 1.4A resolution
4QT3 · FK506-binding protein (fkbp)-type peptidyl-propyl isomerase: “Crystal structure resolution of plasmodium falciparum FK506 binding domain (FKBP35) in complex with rapamycin…”. X-ray diffraction, 2 ligands (DTV, RAP), 1 pocket (best…
- 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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