Research workbench
Biochemical and structural characterization of a divergent loop cyclophilin from caenorhabditis elegans
Analyse Biochemical and structural characterization of a divergent loop cyclophilin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DYW
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclophilin 3
- EC
- 5.2.1.8
- UniProt
- P52011
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclophilin 3 (EC 5.2.1.8) | protein | 172 | 13% helix, 31% strand | P52011 |
Compared structures
- 1DYW · Biochemical and structural characterization of a divergent loop cyclophilin from… · the same entry in another collection · chain A against A, TM-score 1.00
- P52011 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase 3 (P52011) · 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 P52011
- Elsewhere: RCSB PDB 1DYW · PDBe 1DYW · UniProt P52011
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