MolNFT v1 · #19000 · protein
Crystal structure of a truncated form of fkpa from escherichia COLI, in complex with immunosuppressant FK506
1Q6I · Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa: “Crystal structure of a truncated form of fkpa from escherichia COLI, in complex with immunosuppressant FK506”. X-ray diffraction, 1 ligand (FK5), 3 pockets (best druggability…
- PDB
- 1Q6I
- Type
- protein
- Length
- 420 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa
- EC
- 5.2.1.8
- UniProt
- P45523
- Ligands
- FK5
- Pockets
- 3 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fkbp-type peptidyl-prolyl cis-trans isomerase fkpa (EC 5.2.1.8) | protein | 210 | 47% helix, 21% strand | P45523 |
Ligands and binding sites
- FK5 · 8-deethyl-8-[but-3-enyl]-ascomycin · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.38 | 0.75 | 15 | empty |
| 2 | 71 | 0.35 | 0.75 | 12 | empty |
| 3 | 60 | 0.27 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 2291 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 1Q6I · Crystal structure of a truncated form of FkpA from Escherichia coli, in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P45523 · AlphaFold monomer V2.0 prediction for fkbp-type peptidyl-prolyl cis- trans isomerase fkpa… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P45523
- Elsewhere: RCSB PDB 1Q6I · PDBe 1Q6I · UniProt P45523
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