Research workbench
FKBP13-FK506 complex
Analyse FKBP13-FK506 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NNR
- Type
- protein
- Length
- 203 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP2
- EC
- 5.2.1.8
- UniProt
- P26885
- Ligands
- FK5
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP2 (EC 5.2.1.8) | protein | 102 | 9% helix, 36% strand | P26885 |
| B | Peptidyl-prolyl cis-trans isomerase FKBP2 (EC 5.2.1.8) | protein | 101 | 12% helix, 39% strand | P26885 |
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
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.41 | 0.78 | 13 | empty |
| 2 | 73 | 0.37 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 64 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
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 P26885
- Elsewhere: RCSB PDB 4NNR · PDBe 4NNR · UniProt P26885
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