Research workbench
The FK1 domain of FKBP51 in complex with peptide-inhibitor hit dfpfv
Analyse The FK1 domain of FKBP51 in complex with peptide-inhibitor hit dfpfv in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ETV
- Type
- protein
- Length
- 133 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP5; Peptide-inhibitor hit
- EC
- 5.2.1.8
- UniProt
- Q13451
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8) | protein | 128 | 17% helix, 37% strand | Q13451 |
| B | Peptide-inhibitor hit | protein | 5 | 0% helix, 20% strand | — |
Interfaces
1 interface between chains.
- A–B · 370 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7ETV · The FK1 domain of FKBP51 in complex with peptide-inhibitor hit DFPFV · the same entry in another collection · chain A against A, TM-score 1.00
- Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q13451
- Elsewhere: RCSB PDB 7ETV · PDBe 7ETV · UniProt Q13451
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