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Structural and biochemical characterization of a cytosolic wheat cyclophilin tacypa-1
Analyse Structural and biochemical characterization of a cytosolic wheat cyclophilin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HY7
- Type
- protein
- Length
- 181 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase; Cyclosporin a
- EC
- 5.2.1.8
- UniProt
- Q93W25
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 170 | 14% helix, 33% strand | Q93W25 |
| B | Cyclosporin a | protein | 11 | 0% helix, 9% strand | — |
Interfaces
1 interface between chains.
- A–B · 500 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 4HY7 · Structural and biochemical characterization of a cytosolic wheat cyclophilin TaCypA-1 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q93W25
- Elsewhere: RCSB PDB 4HY7 · PDBe 4HY7 · UniProt Q93W25
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