Research workbench
Crystal structure of a single-domain cyclophilin from brassica napus phloem sap
Analyse Crystal structure of a single-domain cyclophilin from brassica napus phloem sap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HMZ
- 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
- EC
- 5.2.1.8
- UniProt
- A0A078GRH6
- Ligands
- MG
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 170 | 14% helix, 31% strand | A0A078GRH6 |
| A | Cyclosporin | protein | 11 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- X–A · 511 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified, 1 d-amino (nonstandard, methylation, D-amino acid).
Compared structures
- 6HMZ · Crystal Structure of a Single-Domain Cyclophilin from Brassica napus Phloem Sap · the same entry in another collection · chain X against X, 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 A0A078GRH6
- Elsewhere: RCSB PDB 6HMZ · PDBe 6HMZ · UniProt A0A078GRH6
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