Research workbench
Peptidylprolyl isomerase, cyclophilin-like domain from brugia malayi
Analyse Peptidylprolyl isomerase, cyclophilin-like domain from brugia malayi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A33
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q27450
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 174 | — | Q27450 |
Compared structures
- 1A33 · Peptidylprolyl isomerase, cyclophilin-like domain from brugia malayi · the same entry in another collection · chain A against A, TM-score 1.00
- Q27450 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase 1 (Q27450) · 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 Q27450
- Elsewhere: RCSB PDB 1A33 · PDBe 1A33 · UniProt Q27450
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